Wednesday, October 31, 2007
Extracted from Nexus Magazine, Volume 11, Number 2 (February-March 2004)
PO Box 30, Mapleton Qld 4560 Australia. email@example.com
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From our web page at: www.nexusmagazine.com
© 2003 by Mark Rojek
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Dexter, MI 48130, US
Telephone/fax: +1 (734) 433 9267
ENZYMES AS THERAPEUTIC TOOLS IN HEALING
Since ancient times, enzymes have unknowingly been involved in treating human ailments. Food consists of protein, carbohydrates, enzymes, fat and fibre, minerals and vitamins. While the properties of enzymes have largely been unknown until recently, results were witnessed and associations of health or disease were made between various plant and animal substances. The healing properties of herbs are primarily attributed to alkaloid or other chemical properties that trigger a response in the body. Invariably, the chemistry of herbs affects metabolic enzyme pathways. The unique substance either inhibits an enzyme or stimulates another to change body chemistry. Some plants have unique essential oils capable of inhibiting or destroying pathogenic micro-organisms due to the disruption of some enzymatic pathway of the organism.Observations of the few (medicine men, shamans and later monks) gave them a certain power over the rest of the population who could not identify which plants caused the healing. This was reserved only for the tribal healer and passed on to the favourites within the tribe. The use of hallucinogenic plants was often employed by shamans to elicit the wisdom from the spirit world to aid in the cure of the person. In today's world of organised medicine, control over one's health is still largely in the hands of the elite few and knowledge is kept from the populace. Contrary to the enlightening herbs of the shaman, a moderate number of health care workers become addicted to or self-medicate with pharmaceutical drugs or turn to alcohol to help relieve stress involved in their profession.1, 2, 3
Within the realm of natural medicine, old and new alike, therapies abound. Everything from acupuncture, botanicals and nutrition to homoeopathy and, more recently, "energy medicine" is available to the average patient. Regardless of the modality chosen, what remains to be understood is that in every case the healing can only occur if the body has enough metabolic enzymes to do the work. Enzymes do work. Work in this case denotes the ability to initiate, alter, speed up or slow down biochemical processes. It indicates having the capacity to break apart or join components together synergistically to change their original structure and function. Food is broken down during digestion and made into smaller components which are then utilised in the body for structure and function. Protein is rendered into amino acids and smaller peptides. These can be used as neurotransmitters for proper brain function. Certain amino acids are used for energy, mineral transport and repair of tissue.
Nutrition, as defined by Webster's Third International Dictionary of the English Language, is "The science of food and the processes by which the organism ingests, digests, absorbs, transports, utilizes and excretes food substances". All too often, this definition is forgotten in the field of nutrition. Nutrition today is practised in much the same way as the pharmaceutical drug approach: for every symptom, there must be a deficiency; simply give the mineral or vitamin and the signs will go away. One of the most common assumptions in both allopathic and complementary medicine is that the patient's digestive system is working fine. Unless the patient complains of heartburn, gas, bloating, belching or pain in the abdomen, doctors assume no problems. Divergent to this is the approach Dr Loomis took in his research into enzymes.
Diet, Digestion and Detoxification
When Dr Loomis began his exploration into the benefits of enzymes in restoring health, he knew the starting point had to be with diet and digestion. The dramatic increase in obesity, cardiovascular disease and diabetes in Western societies is evidence of the simple fact that people eat too much. It also reveals signs of chronic enzyme deficiencies. The combination of simple carbohydrates, fats and sugars found in "fast food" are the major contributing factors to the above disease conditions. Food is much more than just a quick fix for energy. Food is responsible for tissue repair and growth, hormone production, eyesight and immune function. Through protein neurotransmitters, food, or the lack of it, affects our feelings, thoughts and behaviour. In her groundbreaking book, Molecules of Emotion, Dr Candace Pert recounts her discoveries of several biochemicals involved with emotions.4 The body requires "raw material" from which to produce these biochemicals. Food is the raw material in the form of protein, fats and carbohydrates. We must appreciate the dynamics of our body's internal environment—the intracellular and extracellular fluid—in order to understand other complications as the result of poor digestion. Intracellular fluid is found inside the cell and is not constant; it changes due to the extracellular fluid—the fluid outside the cell. Intracellular fluid represents about 66% of the water found in the body. Extracellular fluid roughly makes up the other 33% of the body's water. It serves as a means of transport for nutrients and waste products from normal metabolism. The extracellular fluid needs to remain reasonably stable regarding volume (amount of water), temperature, acid-alkali balance (pH) and levels of nutrients (protein, cholesterol, minerals, glucose) to nourish the cells.
The body continually identifies deficiencies and excesses of specific nutrients or metabolic waste products. All attempts are made to rectify any imbalance by changing the chemistry. The hypothalamus is the only part of the brain not isolated by the blood-brain barrier. This barrier shields fragile tissues of the brain from changes in the body's extracellular fluid. It monitors the body's chemistry 24 hours a day, seven days a week. It reads the slightest alteration in the blood, then quickly sets about to make the necessary changes to maintain homoeostasis (balance). The chemistry of the blood is largely determined by what we consume. Food and drink comprise varying combinations of proteins, fats, carbohydrates and fibres, enzymes, vitamins and minerals. It is all about chemistry. The hypothalamus must ascertain how to keep the body in balance despite the type of food consumed. The sort of balance necessary for optimal health for one person may not be the same for another. Indeed, most often they can be radically different. As Shakespeare wrote, "One man's meat is another's poison".
If you cannot completely digest what you eat, several things may happen.
• Firstly, the undigested food remnants pass through the brush-border of the intestinal tract into the blood and lymphatic systems. White blood cells are stimulated to find the offending material and finish breaking it down. This is known as digestive leukocytosis. It is an automatic response every time you eat cooked/processed food. It was thought to be a "normal" reaction to eating, ever since the early 1800s. However, it was shown to be an unnatural response in the 1930s by Dr Paul Kautchakoff.5 He proved by careful monitoring of patients' blood that only cooked—not raw—foods caused the reaction.
• Secondly, the body may begin to consume more than is necessary. Overeating is one way of compensating for deficiencies of nutrients. The deficiencies are not due to the conscious restriction of a particular food. As stated previously by Dr Howell, cooking food destroys all enzymes, thus food will not be entirely broken down into the micronutrients necessary for cellular utilisation. It is like taking something the size of your house down to the size of a grain of sand in order to get inside the cell to nourish it. Enzymes are the only material capable of splitting food into usable nutrients. Given that undigested food cannot adequately nourish cells, the brain will direct the person to eat more of something to make up for what the body did not get from partial digestion. When this happens over long periods, weight gain occurs with continued loss of metabolic enzymes.
Food cravings are another sign of incomplete digestion. What we crave tends to be the food we do not digest very well. The hypothalamus dictates what we eat based on the chemistry of the blood. So when we eat a particular food and have cravings for it later, it is a sign we did not digest it very well. We will continue to eat more of it because there is something in that food we need but did not get. It has been suggested we are craving the enzymes inherent in that food before it was heated. Those enzymes we are chronically missing normally would be found in the food we crave. Dr Howell noted that animals fed cooked/processed food often resorted to eating their own feces. He found it was to replace the food enzymes lost in the cooking process. The enzyme amylase is a good example of the above. Amylase is one of the major carbohydrate- digesting enzymes. It is found in the kernels of grains and in starchy vegetables. By cooking those foods, amylase is destroyed and our body must secrete amylase from other organs, such as the salivary glands. Amylase is known as an IgG histamine blocker. It stabilises the mast cells and basophils that release histamine at the start of inflammatory conditions. One could say amylase is the body's own natural antihistamine. Antihistamines are prescribed for allergies, dermatitis and other histamine-type reactions.
It has been observed clinically that people who eat excessive amounts of simple carbohydrates most often are those with histamine-related health problems—airborne allergen reactions, allergic reactions to insect bites and bee stings, sinusitis and other eye-, ear- and nose-related health issues. Sinus or frontal headaches are frequently associated with chronic amylase deficiency. In Western society, patients with fibromyalgia tend to have a history of excessive intake of refined carbohydrates. Aside from the occasional discussion, there is little distinction made in the general media between simple and complex carbohydrates. People choose what is convenient. The fast food industry is based on this notion of convenience. However, when closely examined, most of what is considered convenient has detrimental effects on our health. The excessive consumption of carbohydrates will cause chronic depletion of amylase. This may result in the typical histamine conditions and pain found in fibromyalgia.
It is also thought fibromyalgia is related to excessive waste in the body. Undigested remains of disproportionate carbohydrate consumption can accumulate in tissue, since the body cannot eliminate it properly. This might partially explain the patient response to palpation at several lymphatic trigger points when being diagnosed. The lymph system removes waste from the body. Yet, this will not occur very well when too much food is eaten, causing a virtual backing up of the "plumbing". Using highly concentrated enzymes with patients who have histamine reactions alleviates the response within a very short time and without the side effects associated with conventional antihistamines. Thirdly, undigested food allows parasites and other pathogenic micro-organisms to live off the waste inside the body. Incomplete digestion allows bacteria to ferment carbohydrates and putrefy protein, giving off gas. The bloating that occurs after meals is the result of this. It is trapped gas, unable to move through the colon. The accumulation of undigested food in the intestinal tract leads to intestinal toxaemia. It is also known as indicanuria and is responsible for a number of health-related problems.
Eliminating Nutritional Stress
In the field of enzyme nutrition therapy, it is not just a matter of supplementing with concentrated enzymes. It is equally important to make the necessary dietary modifications limiting the intake of those foods known to be dietary stress factors for each individual patient. This is determined through a 24-hour urinalysis and Digestive Challenge Test© as developed by Dr Loomis. It is believed that the only real disease is stress. It is how the body reacts to stress that determines what signs and symptoms of disease manifest in the body. Within Dr Loomis's system, we work with the following:
• Modifying diet to reduce dietary stress factors;
• Greatly improving digestion through intake of plant-based enzymes;
• Improving bowel elimination by nutritionally supporting those organs involved;
• Stopping or reducing inflammation;
• Improving immune function with concentrated enzymes;
• Supporting the autonomic nervous system with acidic/alkaline minerals;
• Nutritionally supporting the endocrine system for proper hormonal production.
There is a type of domino effect involved here. By improving dietary intake, you eliminate nutritional stress. Using plant-based enzymes with meals, the nutrients from food will be better digested, transported and utilised and waste will be more easily eliminated. When food is more completely digested, the body gets the nutrients rather than the pathogenic organisms.
Improving bowel elimination ensures a reduction in toxins being re-absorbed through the bowels back into the blood and lymph systems. This also prevents unwanted growth of pathogenic organisms.
Inflammation can be caused by irritation from undigested food both within the gut and in its passage into the surrounding tissue. Leaky gut syndrome is the current name given to this phenomenon. The one area where enzymes show consistent results is in reducing inflammation. Well-documented studies indicate enzymes resolve inflammation and pain in half the normal time.7, 8, 9 If chronic inflammation exists anywhere, the body develops stress in its attempts to resolve it. Over time, this exhausts the adrenals and our immune system, making it easier for detrimental outside influences to affect the body adversely.
Enzymes in Cardiovascular Disease
Cardiovascular disease is the leading cause of death in the Western world. It is amazing that the dietary link still evades the medical community. Doctors pay lip service to a "healthy diet" and exercise as preventive measures. Dietitians have even worked out a "food pyramid" to help us make wise eating choices. Yet, in spite of the best intentions, the death rate continues to rise and there is no chance of its diminishing in the near future based on the models we have. The food industry "fortifies" food with some 11 "essential" nutrients including B vitamins, calcium, magnesium, potassium, iron and sodium. Yet, the very substances that would digest the food are deliberately left out, destroyed for the sake of extended shelf life.
At the beginning of the 20th century, the transportation of food across a continent posed serious problems. How could a company ship raw, uncooked food without spoilage? The answer was to find a way to process the food and ship it without rotting. In the early 1900s, salicylic acid (aspirin) was used because it "prevented the action of enzymes (unorganised ferments), like diastase, emulsion, and that of mustard, also gastric digestion, fermentation by yeast, ammoniacal fermentation of urine and the germination of seeds".10 In other words, salicylic acid was "distinctly antagonistic to most enzymes".11
So as early as 1903, aspirin was known to affect enzymes. It was used in this way to preserve food for extended shelf-life. As newer techniques for extending the shelf-life were discovered, aspirin was discontinued. Is it not puzzling, then, knowing how aspirin destroys most enzymes, that many patients are told to take aspirin in the prevention of heart disease? From the same reference, it is stated that salicylic acid "has a disintegrating action on the blood corpuscles".
The blood-thinning properties of aspirin result from the fact that it destroys red blood cells, causing fewer of them to be found in the bloodstream! The medical explanation of cardiovascular disease fails to explain the picture fully because it is missing the major piece of the puzzle. Medical research is funded with billions of dollars to find the "cure". In spite of this, triple-bypass surgery is covered by insurance while the advice and wisdom of nutritionists is not. Prevention is not practised because it does not bring in the revenue that surgery, radiation and drugs do. Much attention is paid to markers of potential heart disease. The category of lipoproteins is a good example. Lipo means "fat", and protein is self-explanatory. The four principal classes are: high density (HDL), low density (LDL), very low density (VLDL) and chylomicrons. Chylomicrons are dietary triglycerides. VLDLs are endogenous (from within the body) triglycerides, while LDL and HDL are both endogenous cholesteryl esters. Lipoproteins are necessary for the transport of lipids (fats). We are told it is healthy to have relatively high HDL levels, but should have low cholesterol (LDL), VLDL and triglyceride levels.
The endogenous group of lipoproteins is manufactured within the body, but the raw material is still derived from the fats and proteins we consume. Food must be digested in order for the body to utilise it. The abnormal accumulation of lipoproteins in the blood in a small percentage of the population represents an autosomal dominant genetic trait. But in the majority of people with cardiovascular issues, it is evidence of incomplete digestion of fats and protein—accompanied by the fact that people simply overeat. How can the body properly eliminate unused fats and protein when there simply is too much being taken in? The body must hide or store this unusable waste. Some of it is stored in tissue and some of it circulates. When the kidneys and colon cannot eliminate enough waste, the skin compensates. The skin is the largest eliminative organ. Skin eruptions are the attempts to rid the body of waste.
Unfortunately, what circulates begins to adhere to the walls of the blood vessels, clogging them up. Macrophages are summoned to remove this accumulation, but cannot do so without an adequate supply of enzymes. Enzymes produced by the macrophages for their immune function are believed to be shifted to digesting the cooked food. Obviously, this prevents the breakdown of lipoproteins which continue to build up. Foam cells associated with atherosclerosis are formed when overaccumulation of fats occurs in macrophages.12, 13, 14, 15
Why has no one asked how this accumulation occurs? What is the bigger picture? It is this author's opinion that the accumulation transpires because cooked foods are not completely digested in the stomach. These undigested remnants cross the intestinal border into the blood and lymph, circulating throughout. Over time, their accumulation leads to damaged arterial tissue. Macrophages cannot break down the lipoproteins due to the exhaustion of their own enzymes. Eating cooked fats demands enzymes digesting them. Cooked foods must be broken down, even at the expense of the cardiovascular system. This daily assault of cooked foods drains lipase from many sources, especially the immune and lymph systems. Plant enzymes taken before meals completely digest food. Therefore, no remnants can cross over into the blood. Having prevented further accumulation of undigested food, one can focus on removing the accumulated material. Enzymes taken in between meals are taken up by the body and sent to work in areas that need them the most. Enzymes will digest the undesirable lipoproteins in the blood vessels without affecting the vessels themselves. Reversal of cardiovascular disease is a matter of improving digestion and modifying dietary stress factors—in this case, fats and proteins.16, 17, 18, 19
Enzymes and Immune Function
When metabolic enzymes have been constantly drained from other organs and systems (particularly the immune system) to digest cooked food, there will be little left during an immune crisis, as in fever. Regrettably, sometimes the temperature from a fever rises too rapidly, causing great distress, such as seizures in children. If there is the risk of febrile seizure in a child, suppressing the fever with drugs such as ibuprofen or acetaminophen initially may be the wise thing to do; but these drugs are known to suppress immune function. Thus, preventing a febrile seizure first and then enhancing immune function through natural means would ensure a speedier recovery. Consulting a physician is advisable in this case. Someone not prone to febrile seizure may be carefully monitored to allow a fever to take its course but should be given plenty of fluids. Supplemental proteolytic (protein-digesting) enzymes enhance immune function, helping to destroy pathogens. These may help put an end to a fever more rapidly, significantly boosting immune function by destroying the offending pathogen.
Drinking sufficient water helps keep in check the "fire" induced by a fever. It also provides necessary moisture for enzymes produced by immune cells to defend the body. During a fever, extreme hot or cold weather conditions and strenuous exercise, enzymes are used up at a much faster rate. Becoming dehydrated due to decreased water consumption over time and the use of dehydrating agents such as caffeine and alcohol may make it more difficult for the body to resolve many of the health crises. It is believed that using supplemental enzymes during a fever augments available enzymes from white blood cells to destroy foreign micro-organisms rapidly. Taking exogenous enzymes during a fever can dramatically improve immune function, resolving a fever more quickly.
A fever's typical temperature range of 99–105°F [37.22–40.56°C] is at the high end of plant enzymes' optimal temperature range. Throughout a fever, enzymes in blood and tissue increase as defence mechanisms and for the removal of waste. Moreover, they are used up at a much faster rate. A fever is the body's way of destroying pathogenic micro-organisms through heat and increased enzyme activity. Phagocytosis is a process where macrophages surround and engulf pathogens. They secrete enzymes which digest the invading pathogen. Referring to digestive leukocytosis, when cooked food remnants cross the brush border of the intestine into the blood, leukocytes are activated to find and finish digesting those food components in the blood. When this occurs repeatedly over time and from one generation to the next, the results are compromised immune systems. This is due to the loss of enzymes from white blood cells, which sacrifice them for digesting the food we eat. Note that Dr Pottenger's cats study showed an increase in disease from one generation to the next, and that cancer rates have continued to soar despite the "War on Cancer".
After researching library archives on the clinical use of enzymes as far back as the early 1900s, specifically the work of Dr John Beard and later that of Dr Howell, this author cannot help but ask the following questions: What if one of the pancreas's chief roles is that of an "immune" gland as well as a digestive one? What if Dr Beard's observations of the pancreas-producing enzymes destroying pre-cancerous cells (trophoplasts) are correct? One study investigated the stimulation of "digestive enzymes" of the pancreas of rabbits after exposure to histamine.20 Histamine is one of the major components of the inflammatory response in mammals. Is it possible that the term "digestive enzymes" in this case is incorrect? Are enzymes produced by such a reaction necessarily digestive, or are they responding to resolve the inflammation? Enzymes are known to speed the process of inflammation, thereby resolving it more rapidly.21, 22, 23, 24, 25 If the pancreas responds to histamine by producing enzymes, could they be for healing the damaged tissue and stabilising the mast cells and basophils that released the histamine in the first place?
Proteases (proteolytic enzymes) are known to mediate the defence mechanisms of the body and maintain homoeostasis. It is theorised that proteolytic and other enzymes work in two ways as part of the body's immune system. Firstly, orally ingested enzymes are believed to be marked by the body as "self" and, like the character in the video game "Packman™", are capable of digesting foreign proteins in the body that are "not-self". This would include foreign protein in the form of undigested food remnants, bacteria, viruses and other micro-organisms. Secondly, exogenous enzymes taken away from food are thought to be absorbed across the intestinal lumen and transferred into the blood, where white blood cells uptake them to be used in a variety of activities. Numerous studies have been conducted in enzyme research that point to the benefits of exogenous enzyme therapy in many immune system–related diseases. Allergies, cancers, so-called auto-immune diseases, HIV and other viral diseases, bacterial infections and fungus/yeast infestations have all been shown to be helped by enzyme therapy.26, 27, 28, 29
In the event of allergies, enzymes break down the allergen/antibody complex, splitting it away from surrounding tissue when involved. Enzymes then break down the allergen into smaller components capable of being eliminated without stressing the body. Airborne allergens typically contain both protein and polysaccharide (complex sugar) structures. After entering the bloodstream, they normally are cleaved by enzymes secreted from white blood cells. In an allergic reaction, however, there may not be enough enzymes available from white blood cells to do the work, leaving the mast cells and basophils to release histamine. There occurs the typical allergic reaction of runny nose, swollen itchy eyes, pain, heat and redness in the area of reaction. In a study from Germany, enzymes were shown to split circulating immune complexes as measured in decreased values in blood and improvement of clinical symptoms.30 Several attempts have been made in using protease enzymes for patients with coeliac disease, but with little success. It had been thought that the gliadin protein structure of many grains such as wheat, rye, barley and oats was to blame for the violent reactions suffered by patients. In a study on coeliac disease, the carbohydrate portion was removed with carbohydrases, resulting in total success. There was no damage to the intestinal mucosa as there usually is in this disease.31 Furthermore, the protein portion was not altered. This shows once again the specificity of substrate which enzymes display.
One of the exciting factors resulting from enzyme therapy comes from a study out of Austria.32 It was shown that pancreatic enzymes as well as the constituents bromelain and papain stimulated the production of tumour necrosis factor. Tumour necrosis factor is a cytokine (a non-antibody protein which act as an intercellular mediator in an immune response) capable of haemorrhagic necrosis (destruction) of tumours and can exert cytostatic and cytotoxic activity on transformed cell lines. In other words, enzymes not only digest foreign objects but they can activate other protein products of the immune system to destroy undesirable growths in the body. Although the above references represent only a small number of studies, it can be seen that enzymes have a therapeutic role for many disorders. Other studies include treating autism, sports injury, herpes infection, cancer and auto-immune disease.33, 34, 35, 36, 37
Supplemental Enzymes for Health and Longevity
While changing over to a raw food diet (or nearly an all raw food diet) is desirable, this requires discipline. Each one of us should take the leap into the world of raw food and experiment to find out what works for us. One can find safe, natural animal products to be used for protein intake. The best proponent of this is Aajonus Vanderplanitz. His website, http://www.primaldiet.com, details his experiences over a lifetime of experimenting with raw foods, especially raw animal products. There are numerous other raw food advocates located on the Internet and they have written several books, primarily dealing with a vegetarian raw food diet. Each has their arguments and points of view. In the end, it is the reader who must decide after experiencing what they believe to be in their own best interest. Whether to be a vegetarian or not is finally decided through trial and error and education. How you feel physically, spiritually and emotionally should be noted during any transition. The impact on one's health using enzymes can only be experienced to be appreciated. We are born with enzyme deficiencies, and we have a limited potential for producing enzymes. Dr Howell believed supplemental enzymes are important not only for health and longevity but as a type of insurance. As we grow older, our bodies do not produce as many enzymes as when we were children or young adults. What better way to ensure our health into old age than to eat enzyme-rich foods and supplement with enzymes where needed?
Clinical studies are generally funded by the pharmaceutical companies for the profits of shareholders, and tend not to be conducted for purely altruistic reasons. Furthermore, there is little interest in natural products because they cannot be synthesised and patented—at least not in the USA.
We are living in quite a crazy world where anyone can buy and implement various biological and chemical threats. Anthrax and smallpox are only the tip of the iceberg of the dangers we face.
As has been written in previous issues of this magazine, there are forces interested in creating chaos—only to hand us a solution, but at a very great trade-off. I believe that enzymes offer mankind the greatest hope of preventing and treating the threats we may face in the coming years. I also encourage you to take up this call to educate yourself in all available material from reliable sources to keep your family and loved ones safe and healthy. ∞
About the Author:
Mark Rojek began researching alternative therapies in 1970. His studies included botanicals, mineral and vitamin requirements and diet. He interned in acupuncture with Dr Bell in Windsor, Ontario, Canada, in 1973, and graduated in 1978 with a Bachelor of Science. He studied aromatherapy, kinesiology, massage therapy and classical homoeopathy in England. In 1986, Mark began formal studies in traditional Chinese medicine, especially acupuncture. In Chicago, he worked with several holistic physicians as a medical technician and maintained a private nutritional practice. Also in 1986, he met Dr Howard Loomis, foremost living expert in enzyme nutrition, and continues to work with him. He works with several doctors in Michigan who refer to him and seek his counsel. He continues to research, lecture and counsel clients in nutrition and diet.
• Beazell, J.M. et al., "A Reexamination of the Role of the Stomach in the Digestion of Carbohydrate and Protein", Am. J. Physiology 132:42-50 (1941)
• Howell, E., Enzyme Nutrition, Avery Publishing, New Jersey, 1985
1. Flaherty, J.A., Richman, J.A., "Substance use and addiction among medical students, residents, and physicians", Psychiatr. Clin. North. Am. 16(1):189-97 (1993 Mar)
2. Wolfgang, A.P., "Substance abuse potential and job stress: a study of pharmacists, physicians and nurses", J. Pharm. Mark. Manage. 3(4):97-110 (1989)
3. Rosvold, E.O., Vaglum, P., Moum, T., "Use of minor tranquilizers among Norwegian physicians. A nation-wide comparative study", Soc. Sci. Med. 46(4-5):581-90 (1998 Feb-Mar)
4. Pert, Candace B., Molecules of Emotion: The Science Behind Mind-Body Medicine, Touchstone, 1999, Simon & Shuster, New York, 1997
5. Kouchakoff, P., "The influence of food cooking on the blood formula of man", Proceedings: First International Congress of Microbiology, Paris, 1930, translation by Lee Foundation for Nutritional Research Milwaukee, WI, USA
6. Loomis, H.F., Jr, Enzymes: The Key to Health – Volume 1: The Fundamentals, 21st Century Nutrition, Madison, WI, USA, 1999
7. Blonstein, J.L., "Oral enzyme tablets in the treatment of boxing injuries", The Practitioner 198:547-48 (1967 Apr)
8. Buck, J.E., Phillips, N., "Trial of Chymoral in professional footballers", Brit. J. Clin. Prac. 24(9):375-77 (1970 Sep)
9. Boyne, P.S., Medhurst, H., "Oral anti-inflammatory enzyme therapy in injuries in professional footballers", The Practitioner 198:543-46 (1967)
10. Loomis, ibid.
11. Loomis, ibid.
12. Nakamura, R., Ohta, T., Ikeda, Y., Matsuda, I., "LDL inhibits the mediation of cholesterol efflux from macrophage foam cells by apoA-I–containing lipoproteins. A putative mechanism for foam cell formation", Arterioscler. Thromb. 13(9):1307-16 (1993 Sep)
13. Vainio, S., Ikonen, E.; "Macrophage cholesterol transport: a critical player in foam cell formation", Ann. Med. 35(3):146-55 (2003)
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15. von Eckardstein, A., "Cholesterol efflux from macrophages and other cells", Curr. Opin. Lipidol. 7(5):308-19 (1996 Oct)
16. Hall, D., Zajac, A., Cox, R., Spanswick, J., "The effect of enzyme therapy on plasma lipid levels in the elderly", Atherosclerosis 43:209-15 (1982)
17. Setälä, K., "The promise of enzymes in therapy of hyperlipidemia", Med. Hyp. 20:287-315 (1986)
18. Bergkvist, R., Svärd, P.O., "Studies on the thrombolytic activity of a protease from Aspergillus oryzae", Acta Physiol. Scand. 60:363-71 (1964)
19. Kiessling, H., Svensson, R., "Influence of an enzyme from Aspergillus oryzae, Protease I, on some components of the fibrinolytic system", Acta Chem. Scand. 24:569-79 (1970)
20. Liebow, C., Franklin, E. Jr, "Histamine stimulation of digestive enzyme secretion by in vitro rabbit pancreas", Digest. Dis. and Sci. 27(3):234-241 (1982 Mar)
21. Tarayre, J.P., Lauressergues. H., "Advantages of a combination of proteolytic enzymes, flavonoids and ascorbic acid in comparison with non-steroid anti-inflammatory agents", Arzneim-forsch./Drug. Res. 27(I):1144-49 (no. 6, 1997)
22. Sol, S., Fletcher, A.P., "Proteolytic enzymes: A therapeutic evaluation", Clin. Pharm. and Ther. 1(2):202-26
23. Duskova, M., Wald, M., "Orally administered proteases in aesthetic surgery", Aesthetic Plastic Surgery 23(1):41-4 (1999)
24. Lie, K.K., Larson, R.D., Posch, J.L., "Therapeutic value of oral proteolytic enzymes following hand surgery", Arch. of Surgery 98(1):103-4 (1960)
25. Woolf, R.M., Snow, J., Walker, J.H., Broadbent, T.R., "Resolution of an artificially induced hematoma and the influence of a proteolytic enzyme", J. of Trauma 5(4):491-94 (1965)
26. Goldberg, D.M., "Enzymes as agents for the treatment of disease", Clinica Chimicia Acta 206:45-76 (1992)
27. Rockwell, G.E., "The effects of enzymes on ragweed-pollen and studies on the iso-electric point of low-ragweed antigen", J. Immunology 41:225-232 (1941 Jun)
28. Stauder, G., Ransberger, K., Streichhan, P., Van Schaik, W., Pollinger, W., "The use of hydrolytic enzymes as adjuvant therapy in AIDS/ARC/LAS patients", Biomed. & Pharmacother. 42:31-34 (1988)
29. Leipner, J., Saller, R., "Systemic enzyme therapy in oncology", Drugs 59(4):769-80 (2000)
30. Ransberger, K., "Enzyme treatment of immune complex diseases", Arthritis Rheum. 8:16-19 (1986)
31. Phelan, J.J., Stevens, F.M., McNicholl, B., Fottrell, P.E., McCarthy, C.F., "Coeliac disease: the abolition of gliadin toxicity bt enzymes from Aspergillus niger", Clin. Sci. Mol. Med. 53:35-43 (1977)
32. Desser, L., Rehberger, A., "Induction of tumor necrosis factor in human peripheral-blood mononuclear cells by proteolytic enzymes", Oncology 47:475-77 (1990)
33. Brudnak, M. et al., "Enzyme-based therapy for autism spectrum disorders: Is it worth another look?", Med. Hyp. 58(5):422-48 (2002)
34. Kleine, M.W., Stauder, G.M., Beese, E.W., "The intestinal absorption of orally administered hydrolytic enzymes and their effects in the treatment of acute herpes zoster as compared with those of oral acyclovir therapy", Phytomedicine 2(1):7-15 (1995)
35. Prochaska, L.J., Piekutowski, W.V., "On the synergistic effects of enzymes in food with enzymes in the human body. A literature survey and analytical report", Med. Hyp. 42:355-362 (1994)
36. Qin, X.F., "Impaired inactivation of digestive proteases by deconjugated bilirubin: The possible mechanism of inflammatory bowel disease", Med. Hyp. 59(2):150-63 (2002)
37. Nouza, K., "Outlooks of systemic enzyme therapy in rheumatoid arthritis and other immunopathological diseases", Acta Univ. Carol. [Med.] (Praha) 40(1-4):101-04
Tuesday, October 30, 2007
Valenkevich LN, Iakhontova OI, Shubina ME.
Department of Propaedeutics of Internal Diseases, University, Petrozavodsk.
Klin Med (Mosk). 1996;74(8):46-8.
The paper presents the results of clinical and laboratory studies of lactrase, a drug containing lactase. This agent is recommended for splitting lactic sugar in subjects with appreciably decreased production of endogenous lactase (hypolactasia). Twenty-eight patients with this condition were examined. Manifest clinical symptoms of the condition were observed after loading with 50 g of lactose in all examinees. Addition of 250 mg of lactrase to lactose led to complete clinical compensation of the deficit of endogenous lactase in 75% examinees, and if 500 mg of lactrase was administered, hypolactasia was compensated in virtually all patients. A single intake of 50 g of lactose with lactrase causes a statistically reliable increase of glycemia in such patients. Moreover, a reliable effect of lactrase was observed when measuring galactose in the urine following the lactose test with 250 and 500 mg of lactrase. Our results indicate a high efficacy of lactrase in the treatment of patients with hypolactasia.
Friday, October 26, 2007
Microbial fibrinolytic enzymes: an overview of source, production, properties, and thrombolytic activity in vivo.
College of Life Sciences, Sichuan University, Chengdu, PR China.
Accumulation of fibrin in the blood vessels usually results in thrombosis, leading to myocardial infarction and other cardiovascular diseases. For thrombolytic therapy, microbial fibrinolytic enzymes have now attracted much more attention than typical thrombolytic agents because of the expensive prices and the undesirable side effects of the latter. The fibrinolytic enzymes were successively discovered from different microorganisms, the most important among which is the genus Bacillus from traditional fermented foods. The physiochemical properties of these enzymes have been characterized, and their effectiveness in thrombolysis in vivo has been further identified. Therefore, microbial fibrinolytic enzymes, especially those from food-grade microorganisms, have the potential to be developed as functional food additives and drugs to prevent or cure thrombosis and other related diseases.
Wednesday, October 24, 2007
JOURNAL NAME- Dig Dis Sci
In a double-blind, crossover study, we determined whether microencapusulated pancreatic enzymes reduce postprandial symptoms experienced by healthy volunteers after ingestion of a high calorie, high fat meal. At 7 AM, 18 subjects ingested 185 g of cookies (1196 calories and 72 g of fat) with three pancrelipase capsules or a placebo. The severity of gastrointestinal symptoms and flatus passages were recorded for 15-17 hr, and end-alveolar samples were obtained hourly for 10 hr. Ingestion of pancreatic supplements was associated with a significant (P = 0.049) reduction in bloating over the entire recording period, and with significant reductions in bloating, gas, and fullness during the dinner to bedtime period. Pancreatic supplements had no significant effect on breath H2 or CH4 concentration.
The finding that pancreatic supplements reduce postprandial symptoms in healthy subjects suggests that these supplements also might be beneficial in irritable bowel syndrome.
Tuesday, October 23, 2007
INVENTOR(S)- Psaledakis, Nicholas G.
PATENT NUMBER- 04514388
PATENT APPLICATION NUMBER- 517801
DATE FILED- 1983-07-27
PATENT DATE- 1985-04-30
NUMBER OF CLAIMS- 3
EXEMPLARY CLAIMS- 1
ART/GROUP UNIT- 128
PRIMARY INDUSTRY- 93-01-BK; 93-01-BK
PATENT CLASS- Invention (utility) patent
INVENTOR COUNTRY/ZIPCODE- 01852
ATTORNEY, AGENT, OR FIRM- Gordon, Edward A.
U.S. PATENT CLASS- 424094100O
INTERNATIONAL PATENT CLASS- A61K03754; A61K037547
PATENT REFERENCED BY- 04695458; 04844897
PATENT STATUS INFO- 08/29/89, Expiration Due to Failure to Pay Maintenance
Fees, (EXP); 08/29/89, Expiration Due to Failure to Pay Maintenance Fees,
A method and composition is disclosed for the prophylactic treatment of
cancer tumor cells contained in a host body having a natural immunological
system and wherein the tumor cells have a protective surface resistant to
the immunological system, to prevent or at least reduce further development
of the tumor cells comprising; introducing a solution of a proenzyme and a
pharmaceutically acceptable carrier into the host body adjacent the tumor
cells, the solution having a concentration of the proenzyme at least in
excess of the proenzymes produced by the host body in the area of the tumor
cells, and contacting the tumor cells with the proenzyme whereby the
proenzyme is converted to its active form which reacts with the tumor cell
surface to sufficiently decompose the surface to permit the natural
immunological system to prevent or reduce development of tumor cells.
EXEMPLARY CLAIMS- Claim- 1. A method for the prophylatic treatment of
sarcoma cancer tumor cells in a host body to prevent or at least reduce
further development of said tumor cells comprising contacting said tumor
cells with a proenzyme selected from the group consisting of trypsinogen,
chymotrypsinogen and mixtures thereof in a concentration at least in excess
of said proenzymes produced by the host body in the area of said tumor
Monday, October 22, 2007
Effect of the microbial lactase (EC 184.108.40.206) activity in yoghurt on the intestinal absorption of lactose: an in vivo study in lactase-deficient human
INSERM U.290, Hopital Saint-Lazare, Paris, France.
Br J Nutr. 1990 Jul;64(1):71-9.
Breath hydrogen excretion was measured in eight lactase (EC 220.127.116.11)-deficient volunteers ingesting 18 g lactose in the form of milk, yoghurt and heated yoghurt. Total excess hydrogen excretion (area under curve) was significantly lower after yoghurt and heated yoghurt, than after milk: 103 (SE 29), 191 (SE 32), and 439 (SE 69) respectively (P less than 0.001). The oro-caecal transit time of fermentable components from yoghurt and heated yoghurt (mainly lactose) was longer than that from milk: 165 (SE 17), 206 (SE 19), v. 103 (SE 19) min (P less than 0.01). An intestinal perfusion technique was used in the same subjects after ingestion on two consecutive days of 18 g lactose in yoghurt and heated yoghurt. Significantly less lactose was recovered from the terminal ileum after yoghurt than after heated yoghurt meals: 1740 (SE 260) v. 2825 (SE 461) mg (P less than 0.05), and approximately one-fifth of the lactase activity contained in yoghurt reached the terminal ileum. These findings indicate that more than 90% of the lactose in yoghurt is digested in the small intestine of lactase-deficient subjects and suggest that both the lactase activity contained in the viable starter culture and a slow oro-caecal transit time are responsible for this excellent absorption.
Friday, October 19, 2007
Kuriyama, N.; Kuriyama, H.; Julin, C. M.; Lamborn, K. R.; Israel, M. A.
JOURNAL NAME- Cancer Res
2001 Mar 1
DOCUMENT TYPE- Journal Article
JOURNAL CODE- CNF; 2984705R
JOURNAL SUBSET- MEDJSIM
CORPORATE AUTHOR- Brain Tumor Research Center, Department of Neurological
Surgery, University of California, San Francisco 94143-0520, USA.
PUBLICATION COUNTRY- United States
Effective virus-mediated gene therapy for cancer will be facilitated by
procedures that enhance the low level of gene transfer mediated by
replication-deficient, recombinant viral vectors. We found recently that
protease pretreatment of solid tumors is a useful strategy for enhancing
virus-mediated gene transduction in vivo. In this study, we examined the
potential of protease pretreatment to improve the efficacy of a gene therapy
strategy for prodrug activation that depends on infection with a recombinant
adenovirus encoding herpes simplex virus thymidine kinase (Ad-HSV-tk).
Trypsin or a dissolved mixture of collagenase/dispase was inoculated into
xenografts derived from the human glioblastoma multiforme-derived cell
lines, U87 or U251. Ad-HSV-tk was administered 24 h after protease
pretreatment, and animals were then treated for 10 days with ganciclovir
(GCV). We found that protease pretreatment increased the efficacy of
adenovirus mediated HSV-tk/GCV gene therapy in these experimental tumor
models. Mice receiving Ad-HSV-tk/GCV after protease pretreatment
demonstrated a significantly greater regression of tumors compared with
those treated with Ad-HSV-tk/GCV alone. No adverse effects of protease
pretreatment were observed. No signs of metastasis were seen either by
histological inspection of lymph nodes or by a PCR-based analysis of
selected mouse tissues to detect human tumor cells. Our findings indicate
that protease pretreatment may be a useful strategy to enhance the efficacy
of virus-mediated cancer gene therapy.
Thursday, October 18, 2007
Influence of supplemental enzymes, yeast culture and effective microorganism culture on gut microflora and nutrient at different parts of the rabbit
Samarasinghe, K.; Shanmuganathan, T.; Silva, K. F. S. T.; Wenk, C.
JOURNAL NAME- Asian-Australasian Journal of Animal Sciences
A 10 week experiment was carried out to study the influence of supplemental effective microorganism (EM) culture, yeast culture and enzymes on nutrient digestibility and gut microflora of rabbit gastrointestinal (GI) tract. 24 New Zealand White rabbits, 8- to 9-week-old, were allotted to four dietary treatments; a basal (control) feed, basal feed supplemented with either EM (1%), yeast culture or enzymes (400 ppm). Nutrient flow in digesta and their digestibility at ileum, caecum, colon and in the digestive tract as well as gut microflora distribution were studied. Feed dry matter was diluted from 92% to approx equal to 14% up to the ileum and approx equal to 95% of this water was reabsorbed by the colonic rectal segment followed by caecum (25%). EM and yeast improved protein digestibility at a lower rate than enzymes Ileal, caecal, colonic and digestive tract digestibility of crude protein with enzymes were higher by 10.8, 9.4, 11.3 and 10.7%, respectively, as compared with the control. Yeast and enzymes increased crude fibre digestibility at ileum, caecum, colon and in the digestive tract by 8.5, 9.6, 9.0 and 8.3%, respectively, while EM improved them at a lower rate. Irrespective of treatments, digestive tract digestibility of crude protein (0.698-0.773) and fibre (0.169-0.183) were higher (P<0.05) than the ileal digestibility. Even though a post-caecal protein digestibility was observed, fibre digestion seemed to be completed in the caecum especially with yeast and enzymes High precaecal digestibility of crude fibre (97%) and protein (95%) were observed even without additives probably due to caecotrophy. EM and yeast culture promoted the growth of lactic acid bacteria especially in the caecum but they did not influence gut yeast and mould. The present findings reveal that even though rabbits digest nutrients efficiently through hind gut fermentation, they can be further enhanced by EM, yeast and enzymes Out of the three additives tested, enzyme was found to be the best.
Tuesday, October 16, 2007
Efficacy of oral pancreatic enzyme therapy for the treatment of fat malabsorption in HIV-infected patients
Internal Medicine, University Hospital of Palermo, via Coffaro 25, 90124 Palermo, Italy. firstname.lastname@example.org
Aliment Pharmacol Ther. 2001 Oct;15(10):1619-25.
BACKGROUND: Nutrient malabsorption is a negative prognostic factor in acquired immunodeficiency syndrome and recent studies have shown that pancreatic insufficiency is a codetermining factor of malabsorption. AIMS: To evaluate the effectiveness of open-label oral pancreatic enzyme supplementation therapy in acquired immunodeficiency syndrome patients with fat malabsorption. PATIENTS AND METHODS: Twenty-four consecutive patients with human immunodeficiency virus infection and fat malabsorption were recruited (11 males, 13 females; median age, 9.1 years). Faecal fat loss was evaluated by steatocrit assay at entry to the study (T-0), after 2 weeks (T-1) without pancreatic enzyme treatment and after a further 2 weeks (T-2) of treatment with pancreatic extracts (Creon 10 000 at a dose of 1000 units of lipase per gram of ingested dietary fat). Faecal elastase-1 and chymotrypsin were assayed at entry. RESULTS: Six patients (25%) had abnormally low elastase-1 and/or chymotrypsin faecal concentration. In all patients, steatocrit values were elevated at both T-0 and T-1. Five patients proved intolerant to pancreatic enzyme treatment because of the onset of abdominal pain, and therapy was discontinued. In the 19 patients who concluded the study, steatocrit values during pancreatic enzyme treatment (T-2) were significantly lower than at entry (P < 0.0001). At T-2, in eight of 19 patients, steatocrit values were within the normal limit and the frequency of cases cured or improved on pancreatic enzyme therapy (at T-2) was significantly higher than that observed during the previous study period without enzyme treatment (T-1) (P < 0.01). A positive significant correlation was found between steatocrit values at entry and the Centers for Disease Control class (P < 0.0005); also, the decrease in steatocrit values during pancreatic enzyme therapy (difference between steatocrit value at T-2 and steatocrit value at T-0) positively correlated with the Centers for Disease Control class (P < 0.05). CONCLUSIONS: This pilot, open-label study showed that pancreatic enzyme supplementation therapy is highly effective in reducing faecal fat loss in human immunodeficiency virus-infected patients with nutrient malabsorption. Further double-blind studies must be undertaken to verify these results and, if they are confirmed, pancreatic enzymes can be added to our weapons in the fight against human immunodeficiency virus-associated nutrient malabsorption.
Monday, October 15, 2007
Clinca Medica I, University of Bologna, Italy.
Am J Gastroenterol. 1988 Oct;83(10):1145-9.
The efficacy of lactase by Kluyveromyces lactis in hydrolyzing milk lactose and reducing milk intolerance symptoms was tested in 52 proved lactose malabsorbers. The enzyme was added to milk administered to the patients, and H2 breath excretion (as an index of carbohydrate malabsorption), was determined by gas chromatograph technique, and milk intolerance symptoms were recorded. H2 mean excretion was 78.3 +/- 5.49 ppm after administration of intact whole milk 500 ml (test A), 43.5 +/- 4.99 ppm when lactase 2000 U was added to milk 500 ml immediately before administration (test B); 36.7 +/- 5.01 ppm when milk 500 ml was incubated for 12 h with lactase 1000 U (test C), and 29.7 +/- 4.35 ppm when the incubation was prolonged for 24 h (test D). Symptoms score was: test A = 5.85 +/- 0.56, test B = 3.71 +/- 0.45, test C = 2.77 +/- 0.63, test D = 1.7 +/- 0.68. A correlation index of r = 0.44 (p less than 0.01) was obtained between reduction in H2 mean excretion and reduction in symptoms score of a single individual. The addition of this lactase to milk seems to be effective in correcting lactose malabsorption, thus representing a convenient approach in milk intolerance.
Friday, October 12, 2007
INVENTOR(S)- Maeda, Hiroshi; Matsumura, Yasuhiro; Asami, Osamu; Tanaka,
Hideyuki; Sasaki, Ikuharu
PATENT NUMBER- 04844897
PATENT APPLICATION NUMBER- 906240
DATE FILED- 1986-09-12
PATENT DATE- 1989-07-04
NUMBER OF CLAIMS- 4
EXEMPLARY CLAIMS- 1
ART/GROUP UNIT- 185
PATENT CLASS- Invention (utility) patent
INVENTOR COUNTRY/ZIPCODE- JPX; JPX; JPX; JPX; JPX
PATENT ASSIGNEE(S)- Maeda, Hiroshi; Amano Pharmaceutical Co., Ltd.
ASSIGNEE CITY- Kumamoto; Nagoya
ASSIGNEE COUNTRY- JPX; JPX
ATTORNEY, AGENT, OR FIRM- Wegner & Bretschneider
U.S. PATENT CLASS- 424094300O
U.S. CLASSIFICATION REFS.- X424094630; X435220000; X435221000
INTERNATIONAL PATENT CLASS- A61K03754; C12N00952; C12N00954
PATENT REFERENCE(S)- 3823072; 4066503; 4079125; 4495285; 4514388
PATENT REFERENCED BY- 05856451; 06030933; 06322815
PATENT APPLICATION PRIORITY- 60-201607; 61-184126
PRIORITY COUNTRY CODE- JPX; JPX
PRIORITY DATE- 19850913; 19860807
Method of treating a tumor in a mammal comprises administering to said
mammal an effective anti-tumor amount of proteases originating from
microorganisms. ; Method of treating a tumor in a mammal comprises
administering to said mammal an effective anti-tumor amount of a protease
originating from a microorganism which protease is chemically modified by
one of the following procedures: ; (a) coupling with a saccharide, ; (b)
introduction of a hydrophobic polymeric group, ; (c) alteration of electric
charge of the protein surface, ; (d) conjugation with a low molecular weight
anti-tumor agent of molecular weight less than 2,000, ; (e) formation of
dimer or oligomer by cross-linking of protease molecules, ; (f) conjugation
with a synthetic polycation, ; (g) conjugation with a synthetic polyanion,
and ; (h) combination of the above-mentioned procedures. ; Microorganism
protease is chemically modified by one of the following procedures: ; (a)
coupling with a saccharide, ; (b) introduction of a hydrophobic polymeric
group, ; (c) alteration of electric charge of the protein surface, ; (d)
conjugation with a low molecular weight anti-tumor agent of molecular weight
less than 2,000, ; (e) formation of dimer or oligomer by cross-linking of
protease molecules, ; (f) conjugation with a synthetic polycation, ; (g)
conjugation with a synthetic polyanion, and ; (h) combination of the
EXEMPLARY CLAIMS- Claim- 1. Method for treating a tumor in a mammal which
comprises directly administering into the tumor of said mammal an effective
anti-tumor amount of proteases produced from a source, said source selected
from the group consisting of Serratia marcescens, Bacillus sp. and
Streptomyces griseus, wherein said protease is other than an acid protease .
Thursday, October 11, 2007
1Department of Pediatrics, Faculty of Medicine, Ain Shams University, Abbassia, Cairo, Egypt. Eur J Clin Nutr. 2004 Nov 10; [Epub ahead of print]
BACKGROUND:: Pancreatic exocrine dysfunction has been frequently recorded in protein energy malnutrition (PEM) because the pancreas requires optimal nutrition for enzyme synthesis. This pancreatic enzyme insufficiency may play a role in the continuation of PEM. OBJECTIVE:: This study was designed to assess the pancreatic head size and exocrine pancreatic functions, namely serum amylase and lipase, in PEM and its subtypes and correlate any defect present with the various clinical and laboratory data of the PEM patients with special emphasis on the effect of nutritional rehabilitation. PATIENTS AND METHODS:: A total of 33 cases of PEM; 15 marasmus, 10 kwashiorkor (KWO) and eight marasmic kwashiorkor (MKWO) were recruited from Ain Shams University children's hospital, together with 12 matched controls. The mean age of patients was 11.87+/-7.8 months and that of the controls was 14.83+/-7.7 months. Detailed history taking and thorough clinical examination with special emphasis on anthropometric measurements were taken for each studied infant as well as laboratory investigations which included; complete blood count, liver and kidney functions and serum amylase and lipase. Ultrasonographic assessment of pancreatic head size was performed for the cases and controls. Nutritional rehabilitation program was carried out for 3-6 months followed by reassessment of the cases. RESULTS:: The pancreatic head size values were significantly lower in all subtypes of PEM (1.52+/-0.6, 2.73+/-0.12 and 3.00+/-0.54 cm(3) in the marasmus, KWO and MKWO respectively) compared to the controls (5.13+/-2.33 cm(3)). The serum amylase and lipase were also significantly lower in all subgroups of PEM when compared to the controls with significant improvement following nutritional rehabilitation coupled by a significant increase in pancreatic head size too. No significant differences were recorded when we compared the subgroups together except for a significant higher rate of change in serum amylase in edematous patients compared to nonedematous ones. The length of nutritional rehabilitation period, age of the patient, weight and serum albumin were the most determinant factors for pancreatic head size as evident from the multiple regression analysis study. CONCLUSION:: The potentially correctable exocrine pancreatic insufficiency in cases of PEM should be carefully thought of when planning the nutritional rehabilitation program for such patients as it could be responsible for the serious continued morbidity issues that they face. We thus recommend that estimation of pancreatic head size and exocrine function should be included in the evaluation of PEM patients and they could also be used as a prognostic parameter. SPONSORSHIP:: The patients enrolled were among those admitted and managed freely in the children's Hospital Faculty of Medicine Ain Shams University, including the use of the ultrasound apparatus, while the kits have been purchased by authors who contributed in financing the study.European Journal of Clinical Nutrition advance online publication, 10 November 2004; doi:10.1038/sj.ejcn.1602053.
Wednesday, October 10, 2007
Enzymes are energized protein molecules found in all living cells. They catalyze and regulate all biochemical reactions that occur within the human body. They are also instrumental in digestion. They break down proteins, fats, carbohydrates and fiber making it possible to benefit from the nutrients found in those foods while removing the toxins. Enzymes turn the food we eat into energy and unlock this energy for use in the body. Their presence and strength can be determined by improved blood and immune system functions.
There are three types of enzymes. Our bodies naturally produce two types, digestive and metabolic enzymes as they are needed, while food enzymes can only be consumed orally.
Metabolic Enzymes speed up the chemical reaction within the cells for detoxification and energy production. They enable us to see, hear, feel, move and think. Every organ, every tissue, and all one trillion cells in our body depend upon the reaction of metabolic enzymes and their energy factor. Metabolic enzymes are produced by every living cell. However, the liver, pancreas, gallbladder and other organs play a vital role in their production.
Digestive Enzymes are secreted along the digestive tract to break food down into nutrients and waste. This allows nutrients to be absorbed into the blood stream and waste to be discarded. Human digestive enzymes include ptyalin, pepsin, trypsin, lipase, protease and amylase. The body does not make cellulase, an enzyme necessary for proper digestion of fiber, so it must be introduced through the raw foods we eat.
Food Enzymes are introduced to the body through the raw foods we eat and through consumption of supplemental enzyme fortifiers. Raw foods naturally contain enzymes, providing a source of digestive enzymes when ingested. However, raw food manifests only enough enzymes to digest that particular food, not enough to have support systemically. The cooking and processing of food destroys all of its enzymes. Since most of the food we eat are cooked or processed in some way and since the raw foods we do eat contain only enough enzymes to process that particular food, our bodies must produce the majority of the enzymes we require. For these reasons it is recommended that we supplement our diet with enzymes.
Enzymes Sold in Stores
Plant based Enzymes are the most popular enzymes found in natural food supplements. The four most common are Protease, Lipase, Amylase and Cellulase. They represent about 80% of the market. They are sources from aspergillus and grown in a laboratory setting on plants such as soy and barley. They are called plant based, microbial and fungal. Of all the choices, plant based enzymes are the most active or potent. This means they contain the highest active units and can break down more fat, protein and carbohydrates in the broadest pH range than any other source. Plant based enzymes are useful to develop and maintain a proper digestive system and to allow the body to produce more metabolic enzymes by reducing the need to produce digestive enzymes. They can also be used in varying formulas to treat certain ailments. The other types of enzymes mentioned next are better suited for specific treatment purposes rather than in enzyme maintenance programs.
Aspergillus enzymes have a strong record of safe use in the food industry and are considered food by the FDA. These enzymes can be taken with meals to aid in the digestion of all foods or between meals to feed and fortify the body as a whole. Plant based enzymes are not disposed of as if the body has no need for them, rather they exit only after there is no more left to do their work. Since they are food, which is natural to the body, and since they are the most potent, they are often preferred over other types. The following is a list of other typed of enzymes commonly sold in most health food stores.
Pancreatin is a substance from the pancreas of the hog or ox containing enzymes. Pancreatin contains proteolytic enzymes (enzymes that break down protein), amylase and lipase. This enzyme has been studied extensively for it’s anti-inflammatory properties. Pancreatin has been used successfully in Germany for fortifying the pancreas in a molecular way. Since it is a glandular compound it provides the same type of support a thyroid complex an individual’s thyroid. Dr. Roy Dittnan suggests that pancreatic enzymes should not be taken during pregnancy or when using blood thinners.
Pepsin is a proteolytic enzyme usually prepared from the stomach of pigs and is the principle digestive component of gastric juice. It is usually given to those whose digestion is impaired. However pepsin is only activated at a temperature higher than normal body temperature.
Bromelain is a group of proteolytic and milk-clotting enzymes derived from the pineapple stem. A concentrate of this enzyme can be used as an anti-inflammatory agent, a meat tenderizer, and in the chill proofing of beer. Like pepsin, bromelain is only activated at a temperature higher than normal body temperature.
Papain is a proteolytic enzyme derived from the latex of papaya. This enzyme becomes active in an environment of 6.0-8.0 pH, and requires temperatures above normal human body temperature. For this reason Papain and Bromelain are often used to reduce inflammation since the temperature at points of inflammation are always higher than the rest of the body.
Chymotrypsin is a proteolytic enzyme taken from the pancreas of ox and pigs. This enzyme requires a pH level of 8.0 to become active.
Trypsin is a proteolytic enzyme formed in the intestine and can be taken from the intestine or pancreas of an animal. Trypsin breaks down arginine or lysine and works only in an alkaline setting. Today, it is often coated so that it can make it to the 8.0 pH occurring in the small intestine. It is commonly used to fortify the pancreas and the small intestine.
Enzyme Measurements and Labeling
When comparing enzyme products it is important to note if there are no fillers on the label. Fillers can be many things including leftover fibers or cellulose. Looking at the label of a high quality enzyme product, you will find measurement units you may not be familiar with. These are from the Food Chemical Codex (FCC). The FCC is published by the National Academy Press and is the accepted standard of the U.S. Food and Drug Administration. The system for determining enzyme potency used by the American food industry is derived from the FCC. This is the ONLY National Standard for evaluation of plant enzymes. This system establishes activity levels and potency for enzymes. The following are the most common enzymes used and their FCC abbreviation.
• Alpha-Galactosidase-GALU (Galactosidase Units)
• Amylase-DU (Dextrinizing Units)
• Bromelain-GDU (Gelatin Digesting Units)
• Catalase-Baker Units (named after the author)
• Cellulase-CU (Cellulase Units)
• Glucoamylase-AG (Amyloglucosidase Units)
• Hemicellulase-HCU (Hemicellulase Units)
• Invertase-INVU (Invertase Activity Units)
• Lactase-LacU (Lactase Units)
• Maltase-DP (Degrees of Diastatic Power)
• Nattokinase-FU (Fibrinolytic Units)
• Pectinase-AJDU (Apple Juice Pectinizing Units)
• Phytase-PU (Phytase Units)
• Protease-HUT (Hemoglobin Unit Tyrosine base)
• Xylanase-XU (Xylanase Units)
Is it possible that an enzyme can clean up or purify the blood? When you look at it from the simplest perspective it makes sense. It is a known fact that fungal forms, parasites and bacteria are made up of protein, and the shell that protects a virus in our bodies is in fact a protein coating. The enzyme protease breaks down proteins and since the invaders of our blood systems are protein, it would make sense that ingesting protease on an empty stomach would help purify the blood of protein invaders. An empty stomach is suggested since the protease would not have to be held in the digestive system to digest food protein.
Enzymes in general deliver nutrients, carry away toxic wastes, digest food, purify the blood, deliver hormones by feeding and fortifying the endocrine system, balance cholesterol and triglyceride levels, feed the brain and cause no harm to the body. All of these factors contribute to the strengthening of the immune system.
Break Down Fats
Lipase breaks down (digests) fat. When added to your meal as a supplement it is able to do this in the digestive tract. This takes stress off the gall bladder, liver and pancreas. When taken between meals, they can be of great support systemically and in some cases stored in the liver for later use.
Shed Excess Weight
Many overweight people have a metabolism imbalance or will soon create one. The endocrine system is our metabolism. Once we are able to fortify the endocrine system, get the bowels working regularly, and digest our food rather than turning it into fat, we have a successful combination for losing weight. This process is not instantaneous, because we have to lose fat instead of weight. A person has to lose a great deal of fat to equal one pound of weight. It takes longer, but is healthier and lasts longer. Best of all, it does no harm.
Enhance Mental Capacity
Your body uses glucose called from the liver to feed and fortify the hypothalamus. The hypothalamus directs our endocrine system and is responsible for, among other things, balancing emotions. This long lasting glucose is made from the protein stored in the liver. All plant enzymes come from protein foods, thus they help fortify the liver for this function. Red blood cells carry oxygen and nutrients to the glands, muscles, and all the organs of the body, including the brain. Nutrients however, can only be delivered throughout the body by means of the enzyme delivery system. When this is not accomplished, you become fatigued and are less able to think clearly.
Improved Aging Skin
An adequate supply of enzymes are absolutely essential for keeping your skin young looking and healthy. According to researchers, Amber Ackerson and Anthony Cichoke in Portland Oregon, enzymes fight the aging process by increasing blood supply to the skin, bringing with it life-giving nutrients and carrying away waste products that can make your skin look unhealthy and dull.
Your “Enzyme Potential”
Dr. Edward Howell began researching what he called “Enzyme Potential” in the 1940’s. Since then there has been a great deal of support for this concept.
We all make Digestive and Metabolic enzymes as needed, and it is a proven fact that as we age we make less with each passing year. This ability to make only a limited number of enzymes has been called our enzyme potential. An individual’s potential is dependent on their DNA or what they inherit from their parents. Some people have a great potential. This is exhibited by the quality of their health despite their lifestyle choices. They can essentially eat whatever they want, drink whatever they want, rarely exercise, have high-pressure jobs etc. Despite this, they live long, happy, healthy lives with little illness.
On the opposite side of the spectrum there are people that are essentially born sick. These people have to be careful about every aspect of their lives. To deviate will only bring grief. The difference between these two types of individuals is their enzyme potential. Most of us fall somewhere in the middle of these two groups.
There are three ways to preserve this potential. They are all based on reducing the amount of energy that we spend on digestion. By some estimates, we spend up to 80% of all of the energy we have at our disposal digesting our food. This makes sense since most people require 3 to 10 days to break down, assimilate and excrete the waste of any given meal. Thus our body is in a constant state of digestion. To preserve our potential we need to reduce this amount. One of the easiest ways to do this is to limit the number of digestive enzymes that our body needs to break these meals down. By making less digestive enzymes we will ultimately make more metabolic enzymes in our lifetime. The second choice is to reduce the number of calories we consume. Dr. Roy Walford from UCLA pioneered this concept. By eating less, we are ultimately preserving vital energy (making less digestive enzymes) and again, extending our potential. The third is perhaps the most obvious. Take a high quality digestive enzyme supplement with every meal. The choice is yours!
Have you ever asked yourself, ‘How is it possible that I am sick even though I eat organic foods and am careful with my diet?’ The answer most likely revolves around an ENZYME DEFIECIENY. An enzyme deficiency can manifest itself as a variety of conditions. Presented here is a brief look at causes and symptoms.
Protease digests protein. The benefit of proteolytic enzymes has been studied for decades in the United States, Germany and Japan primarily. Research has focused on immune support, inflammation and cancer.
Since everything that makes us sick is either a protein or is protected by protein, the immune system is constantly in need of protease. Bacteria, parasites and fungal forms are all protein. Viruses and cancer cells are all protected by protein. Protease has the ability to digest this unwanted debris in the blood. Therefore, protease deficient people are immune compromised, making them susceptible to bacteria, yeast and viral infections and a general decrease in immunity.
Amylase digests carbohydrates (converts them into sugars) along with dead white blood cells. When you are low in amylase you are a candidate for blood sugar imbalances, Hypoglycemia, Type II Diabetes, carbohydrate cravings and allergies. Amylase is also involved in anti-inflammatory reactions such as those caused by the release of histamine and similar substances. Asthma and emphysema may also be exacerbated by an amylase deficiency.
Since lipase digests fat, fat-soluble vitamins and balances fatty acids, lipase deficient people can be expected to have a tendency towards high cholesterol, high triglycerides and difficulty losing weight. The future outcome of these tendencies is heart disease, which kills more Americans than any other disease. Lipase deficient people also have decreased cell permeability, meaning nutrients cannot not get in and waste cannot get out. The condition or labyrinthis, also called Meniere’s Disease (dizziness aggravated b movement such as walking or driving), can also result from lipase deficiency.
Cellulase breaks down the fiber in our diet. Because our body does not produce cellulase, this food enzyme is essential. The good bacteria in our intestinal tract has the ability to manufacture cellulase when it is in balance. We can also get it through the raw foods that we eat.
The symptoms of cellulase deficiency can be best described as malabsorbtion syndrome (impaired absorption nutrients, vitamins, or minerals from the diet by the lining of the small intestine). Malabsorption has many symptoms including lower abdominal gas, pain, bloating and problems associated with the jejunum and pancreas. The consumption of fiber enriched nutritional drinks, which are full of cellulose, can exacerbate these problems.
A cellulase deficiency can also lead to fungal overgrowth such as Candida. The cell wall of Candida contains chitin, which is very similar to cellulose (fiber). This can often make it difficult to remove once an overgrowth develops. Cellulase taken orally can often assist in bringing the Candida overgrowth back into balance.
Sucrase, Lactase and Maltase Deficiency:
People who have malabsorption syndrome and cellulose deficiency also have a tendency towards sugar (sucrose, lactose and maltose) and/or gluten intolerance. Sucrose, lactose and maltose are three common sugars, which some people cannot tolerate. They are broken down and absorbed into the system by three enzymes: sucrase, lactase and maltase.
Sucrase deficient cannot split the sucrase disaccharide into twin partners, two units of glucose. Glucose is a primary brain food so expect mental and emotional problems in people who are sucrase deficient. Symptoms include depression, moodiness, panic attacks, manic and schizophrenic behavior and mood swings.
Lactase deficient people also have classic symptoms, which include abdominal cramps and diarrhea. Other allergic symptoms including asthma have been witnessed from the ingestion of lactose containing products.
Maltase deficient people are generally sensitive to environmental conditions.
Intolerance to Sucrose, lactose or maltose may be worsened by a deficiency in sucrase, lactase or maltase.
Combination Deficiency is when an individual has more than one of the above deficiencies. The person will most often have the most severe digestive issues. Crohn’s Disease, Colitis, and Irritable Bowl Syndrome are quite common.
Gluten grains can be a real problem for example. These grains include wheat, oats, rye and barley. Not everyone has to avoid all four grains; however, sometimes it is a must. Gluten intolerance is associated with Celiac Disease and Malabsorption Syndrome. It is also associated with Crohn’s Disease. Gluten is actually a protein that exists in these high carbohydrate grains. The best way to address this is to usually a high potency protease and amylase combination.
The insidious thing about gluten intolerance is that it creates sugar intolerance because when gluten intolerant people eat gluten-containing foods; the brush border cells of the jejunum are injured and thus unable to secrete the disaccharides (sucrase, lactase and maltase) leading to sugar intolerance. The problems discussed here are just the tip of the iceberg. More discoveries continue to emerge as research with food enzymes continues.
Syndromes Common To Enzyme Deficiency
• Breaking out of the skin –rash.
• Hot Flashes
• Cold Hands and Feet
• Neck and Shoulder Aches
• Back Weakness
• Fungal Forms
• High Blood Pressure
• Hearing Problems
• Gum Disorders
• Aching Feet
• Bladder Problems
• Gall Bladder Stress
• Hay Fever
• Prostate Problems
• Chronic Allergies
• Common Colds
• Irritable Bowel Syndrome
• Chronic Fatigue
• Sinus Infection
• Immune Depressed Condition
Therapeutic Uses Of Enzymes
If enzymes truly are catalysts, which participate, in virtually every bodily process, and if a shortage can cause a variety of illness, then why are they not widely used as a treatment? It is certainly true that they are not widely used here in the Americas, but what about other countries? In Europe enzyme therapy is routinely used to treat a variety of illnesses.
As you become familiar and comfortable working with enzymes they will serve you as no other supplementation program. The one thing we must be able to do is digest, assimilate utilize, eliminate and create healthy cells to live. The body requires enzymes to do all this work. If it is true the body uses 80% of its energy just to digest food, there can be no limit to the benefit of plant-based enzymes in this process.
It is known that proteases are able to dissolve almost all proteins as ling as they are not components of living cells. Normal living cells are protected against the lysis by the inhibitor mechanism. Parasites, fungal forms and bacteria are protein. Viruses are cell parasites consisting of nucleic acids covered by a protein film. Enzymes can break down undigested protein, cellular debris, and toxins in the blood, sparing the immune system this task. The immune system can then concentrate its full action on the bacterial, viral or parasitic invasion.
Protease is a polymorphic enzyme. The enzyme action it produces can adapt to meet the current digestive or metabolic needs of the body. It should be noted that protease when taken on n empty stomach is readily taken up into the mucosa cells of the intestine and passed into the blood circulation. Clinical observation (manuscript in preparation have noted that upon high intake of oral protease, heavy metal concentration have been significantly decreased in the blood.
Fats are the most difficult component of the diet to digest. Fatty foods cause more indigestion than protein or starches. Most Americans have crossed wires when it comes to fats. Because of bulging waistlines, most Americans battle between fat-phobia and fat craving. The human body is programmed to crave fats. Without essential fats and fatty nutrients animals and humans cease to thrive. Omega-3 and Omega-6 fats from flaxseeds and cold-water fish were found to be essential for human health by physiologists in the 1930’s. Fat-soluble nutrients such as beta carotene, lutein, and vitamins A, D, E and K fulfill important functions in health maintenance. So fat isn’t all bad.
The American diet is intentionally laden with saturated fats and hardened hydrogenated fats, leaving about 0% of the population deficient in the essential fats required for the maintenance of the human nervous system, the production of hormones and the control of inflammation.
Foods actually taste better when they contain fats. A famous fast-food quarter-pound hamburger actually has saturated fat content equivalent to 16 pats of butter! The fast-food engineers really know how to stimulate our taste buds.
It is worth noting here that weight loss is a common finding among individuals with chronic heart failure. It is evident that malabsorption of fats is related to heart failure. In one study, subjects with heart disease had 10 times more fat in their stool than heart-healthy individuals. This means that those with heart disease weren’t absorbing their fats (AM J Cardiology %: 295, 1960). Yet heart patients are typically placed on low-fat diets! These individuals were leaner, but not healthier.
Foe these same reasons, fat-blockers such as Olean and Elestra are undesirable. They keep fat from being absorbed, but they also keep fatty nutrients from being available. Under-nutrition occurs in about half of the patients with chronic heart failure. Fats are a major source of fuel for the heart muscle. The use of lipase has been suggested to improve fat absorption. (AM J cardiology 8”43,1963).
It was not until1997 that researchers found that lipase also can help to control LDL cholesterol and is helpful in stubborn cases of high triglycerides. ( Lipids 32: 1147, 1997).
Low levels of lipase have been found among adults who have benign fatty tumors surrounding their eyelids, an unsightly condition called xanthelasma. Adults with this condition often hide these fatty growths with make-up. While lipase is untried in these cases, a course of daily lipase with meals may prove to be a remedy.
Plant Based Enzymes vs. Animal Enzymes
Enzymes are the energy of life. All supplemental enzymes, with very rare exception can be beneficial to one degree or another. If you must choose one, which would it be? When considering the benefits of animal (or glandular, usually represented by USP) vs. plant enzymes, the following maybe helpful.
Animal enzymes, or pancreatic enzymes, are from the pancreas of a slaughterhouse animal. Ask yourself “What was the condition of this animal and its organs before it was slaughtered”. How does anyone know?
Pancreatic enzymes tend to claim high unit amounts, such as 31500 units of protease. However, this amount, or unit measurement, does not indicate the actual enzyme activity level. 31500 units of protease will yield a level of only 356 units of digestive activity. Compare this to hundreds of thousands of actual protease activity in our plant based enzymes. Enzyme effectiveness depends on activity not weight. Remember to compare “apples to apples”.
Don’t forget about the importance of the pH balance. Pancreatin requires an 8.0 pH to be of use in the system. The human body reaches this 8.0 pH in the small intestine after major digestion has already taken place. Plant enzymes have the capability to work between 3 and 9 pH. They are blended as neutral, alkaline and acidic to cover all concerns in our formulation. This means they work throughout the entire digestive tract and in the blood. For instance, one English study showed a small dose of acid-stable lipase from a plant source was more effective than a dosage 25 times larger of conventional pancreatin in the treatment of malabsorption and malnutrition due to pancreatic enzyme deficiency.
Tuesday, October 9, 2007
Smallpox, influenza, chicken pox, measles, mumps, herpes viruses from the common cold to rabies have all been a major cause of human misery and death throughout history. In 1939, using an early electron microscope, researchers were able to “see” a virus for the first time. Like other microorganisms, viruses typically gain entry to the body through epithelial surfaces, usually the:
• Mucous membrane of respiratory tract
• Gastrointestinal tract
• Genital tract
• Conjunctiva (Mucous membrane lining on the inside of the eyelid and outside of the eyeball).
If a virus manages to make it through these physical barriers, it encounters a second line of defenses. These defenses are engaged against anything the body recognizes as foreign. They include phagocytes (literally, “cell eaters”), white blood cells whose job it is to engulf, ingest and eliminate foreign particles, of course, viruses before they can infect any of the body’s cells. Perhaps a billion strong, they constantly circulate throughout the body in the blood and lymph systems.
Many white blood cell types can act as phagocytes, but most important to our story are the macrophages. Macrophages (Greek for “big eaters”) may be mobile, circulating through the blood and lymph fluid, or attached to a particular type of tissue. They devour everything, including viruses and bacteria, as well as dead body cells, dead neutrophils and other debris. Other cells called natural killer cells wander through the blood and lymph fluid looking for abnormal cells, particularly those that are infected by viruses or are cancerous. When they find an abnormal cell, they kill it.
How Viruses Differ From Bacteria
Most of us have the sense that viruses are unique in some way and that the viral infections are not as readily treatable as those caused by bacteria. The key differences between viruses and bacteria are size and structure. Viruses are the smallest known form of life, ten to 100 times smaller than an average bacterium. Bacteria are large enough to carry their own synthetic machinery, and thus can live and reproduce independently of a host cell. Viruses, in contrast, are obligate intracellular parasites (that is, they can replicate only inside a host cell). Viruses carry their genetic information either as RNA or as DNA, but bacteria use only DNA.
The structure of a virus is an exercise in simplicity. The most basic viruses have just two components: a core of genetic material and a protein coat called a capsid. In addition to these components, common to all viruses, some viruses have an outer envelope, consisting of a combination of lipids, proteins or carbohydrates. A complete, fully developed viral particle that contains both genetic material and a capsid coat is called a virion. This economical little structure is capable of doing a great deal of harm by invading and replicating within host cells.
The viral genome (genetic material of all living cells) is contained within chemical structures known as nucleic acids. In human cells, deoxyribonucleic acid (DNA) is used to store genetic information. DNA is organized into segments called genes, each of which contains “instructions” for manufacturing a particular protein, which in turn helps determine cell structure and function. Human cells also contain another nucleic acid, ribonucleic acid (RNA), Which helps carry out the instructions encoded in the DNA.
In contrast to human cells, the viral genome can be written in either RNA or DNA. A virus can have either RNA or DNA but never both. The nucleic acid of a virus can be single or double-stranded. The type of nucleic acid and number of strands in a viral genome are ways we classify viruses.
Viral nucleic acids are recognized by human intracellular mechanisms involved in DNA and RNA replication and transcription. Thus, the viral genome can “hi-jack” the host cell’s replication process, a modus operandi that lies at the heart of a virus’ infectivity.
In some viruses, such as herpes viruses, the capsid is also surrounded by an envelope, similar in lipid structure to cell membranes and, in fact, derived from membranes of the host cell in which the virus was replicated. Viruses with such envelopes are termed enveloped; those with no envelope are termed naked.
The envelope of certain viruses is covered by protein-carbohydrate spikes that protrude from the surface of the envelope, giving the virus something of appearance of a medieval mace. These spikes contribute to the infectious properties of the virus helping the virus attach to host cells or causing red blood cells to clump together.
An enveloped virus and a non-enveloped, or naked virus are contrasted. The envelope itself consists primarily of lipids and is similar in composition to cell membrane. In fact, enveloped viruses derive their envelopes from membranes of the host cells they infect.
Glycoproteins on the surface of viruses apparently act as “recognition factors” that enable the virus to recognize and attach to only those cells within its host range (the range of organisms and cell types it infects). In the case of naked viruses, these glycoprotein recognition factors occur on the capsid itself; in enveloped viruses, they protrude through the envelope to the surface of the virus.
Many viruses, however, encode proteins, which specifically bind either antibody or complement (a complex system of proteins found in normal blood serum that combines with antibodies to destroy pathogenic bacteria an other foreign cells) with viruses, and these may provide protection against attack during the intracellular phase. There is some evidence that these provide protection against direct neutralization.
The protein coat or capsid is made up of a series of repeating subunits known as capsomeres. These consist of one, or very few types of proteins coded by the viral nucleic acid. The type an arrangement of these capsomeres is what gives each virus its characteristic architecture. These capsomeres demonstrate how “economical” the virus is in its structure and function. While human cell membranes have hundreds of different structural elements, the viral capsid consists of just a few proteins, repeated again and again. Thus, relatively little of the virus’ genetic material is devoted to coding for these structural proteins allowing the virus to carry a minimum of genetic material.
Proteases & The Protein Coat
Protease is a classification of a group of enzymes which act on protein molecules and assist by catalyzing reactions. These reactions, in effect help to change the molecular structure, or breakdown the protein molecules. Based on clinical studies, it is known that proteases are able to hydrolyze almost all proteins as long as they are not components of living cells or are in an environment that stabilizes their confirmation. Normal living cells are protected against lysis by the inhibitor mechanism. Parasites, fungal forms, and bacteria are protein. Viruses are cell parasites consisting of nucleic acids covered by a protein film. The introduction of oral proteases, presents the ability of those enzymes to act upon the protein coating of viruses. Enzymes can also break down undigested food protein, cellular debris, and toxins in the blood, sparing the immune system this task. The immune system can then concentrate its full action on the bacterial or parasitic invasion.
Protease will hydrolyze various forms of protein that have lost their native stability in the system (waste). The enzyme action it produces can adapt to meet the current digestive or metabolic needs of the body. It should be noted that some proteases when taken on an empty stomach is readily taken up into the mucosa cells of the intestine and passed into the blood circulation. Clinical observations (manuscript in preparation) have noted that upon high intake of oral proteases, heavy metal concentrations have been significantly decreased in the blood.
Oral proteases taken on an empty stomach have been shown to be absorbed and carried into the blood stream where they are bound to alpha-2 macroglobulin. The binding of the alpha-2 macroglobulin to proteases does not inactivate the proteolytic activity of the protease. However, the complexing of the alpha-2 macroglobulin ensures the clearance of the protease from the organism. Several studies have indicated that oral proteases bound to the macroglobulins hydrolyze immune complexes, proteinaceous debris, damaged proteins, and acute phase plasma proteins in the blood stream. It is suggested that oral proteases may help hydrolyze and remove extracellular proteins damaged by free radicals. This is based on the absorbability of the protease into the circulatory system, their hydrolytic activity and ability to remove proteinaceous debris in the blood and extracellular fluid, and their susceptibility due to their unfolding and other conformational modifications from their native state.
To simplify this explanation: It is being suggested that once a virus has been” tagged” by the immune system for elimination from the body, the combination of protease and alpha-2 macroglobulin are able to assist the immune system in breaking down and removing the virus from the system.
Monday, October 8, 2007
Theramedix only uses plant enzymes derived from the fermentation of specific strains of Aspergillus. The Aspergillus used is a “pharmaceutical grade” which establishes their safe use in the production of enzymes, amino acids, and other beneficial compounds.
Enzymes are Isolated Proteins not Living Organisms
Once fermentation by the Aspergillus organism is complete, the enzymes are extracted by a complex process that isolates protein compounds from the surrounding material. No living Aspergillus cells remain in the isolated enzyme after the extraction process is complete.
Infections Associated with Aspergillus
Enzymes derived from the fermentation of Aspergillus are purified compounds, which do not contain any living Aspergillus cells and therefore, cannot initiate infection or colonization. No cases of Aspergillus infections have ever been documented in association with the consumption of purified fermented fungal enzymes.
Allergic Reactions to Aspergillus
Allergic responses to Aspergillus organisms and the products of their fermentation do occur; although their occurrence is largely isolated to regular airborne “dust” exposure by workers in the food industry. If an allergic reaction is to occur, it is generally the protein faction of a substance that will elicit such a reaction. Enzymes derived from Aspergillus fermentation are free of any living Aspergillus cells.