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Dr. Jimmy Gutman, MD, FACEP on Bioactive Whey Protein and Glutathione.

Glutathione FREE report | Glutathione Audio | Glutathione Flash*
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  • WebMD article on Glutathione
  • Nutritional supplements to increase glutathione
  • Foods that are a good dietary source of glutathione
  • The Science of Glutathione.
  • The FDA on Benefits of Glutathione.
  • Glutathione is a substance, the levels of which in our cells are predictive of how long we will live. There are very few other factors which are as predictive of our life expectancy as is our level of cellular glutathione. Glutathione has been called the "master antioxidant", and regulates the actions of lesser antioxidants such as vitamin C, and vitamin E within the body. "We literally cannot survive without this antioxidant," Earl Mindell, R.Ph., Ph.D. "What You Should Know about the Super Antioxidant Miracle"
  • "Without glutathione, other important antioxidants such as vitamins C and E cannot do their job adequately to protect your body against disease." Breakthrough in Cell Defense, Allan Somersall, Ph.D., M.D., and Gustavo Bounous, M.D. FRCS(C)
  • "No other antioxidant is as important to overall health as glutathione. It is the regulator and regenerator of immune cells and the most valuable detoxifying agent in the human body. Low levels are associated with hepatic dysfunction, immune dysfunction, cardiac disease, premature aging, and death." The Immune System Cure, Lorna R. Vanderhaeghe & Patrick J.D. Bouic, Ph.D.
  • Glutathione (L-gammaglutamyl-L-cysteinylglycine) is a tri-peptide of the amino acids cysteine, glycine, and glutamic acid. Glutathione is an antioxidant compound found in living animal and plant tissue. It takes up and gives off hydrogen and is important in cellular respiration. A deficiency of glutathione can cause hemolysis (destruction of red blood cells, leading to anemia) and oxidative stress. Glutathione is essential in intermediary metabolism as a donor of sulfhydryl groups which are essential for the detoxification of acetaminophen. [PDR Medical Dictionary. Spraycar. 1999] Selenium is a structural component of, and a co-factor for the antioxidant enzyme glutathione peroxidase.

    Glutathione is the major endogenous antioxidant produced by the cell. Glutathione participates directly in the neutralization of free radicals, reactive oxygen compounds, and maintains exogenous antioxidants such as vitamins C and E in their reduced (active) forms. In addition, through direct conjugation, glutathione plays a role in the detoxification of many xenobiotics (foreign compounds) both organic and inorganic. Glutathione is an essential component of the human immune response. Proposed mechanisms of immune enhancement include:
    1. optimizing macrophage functions,
    2. offsetting oxidative damage associated with lymphocyte monoclonal expansion, and
    3. stabilizing the mitochondrial membrane thereby, reducing apoptosis in lymphocytes

    glutathione

  • Cysteine is a sulfur-containing (sulfhydryl) amino acid which is present in many proteins, and is in the same class as methionine. Because it is a sulfur-based amino acid, cysteine acts as an antioxidant in the body. Cysteine is an important source of sulfur in human metabolism, and although it is classified as a non-essential amino acid, cysteine may be essential for infants, and may at some point be recognized as an essential or conditionally essential amino acid. The systemic availability of oral glutathione is negligible; the vast majority of it must be manufactured intracellularly. Glutathione (GSH) is a tripeptide made up of the three amino acids cysteine, glycine and glutamate. Glutamate and glycine are readily available in most North American diets, but the availability of cysteine makes it be the rate-limiting substrate for the synthesis of glutathione within the cell. It is the sulfhydryl (thiol) group (SH) of cysteine that serves as proton-donor and is responsible for the biological activity of glutathione.

  • cysteine

    The free amino acid cysteine does not represent an ideal delivery system to the cell. It is potentially toxic and is spontaneously catabolized in the gastrointestinal tract and blood plasma. Conversely, cysteine absorbed during digestion as cystine (two cysteine molecules linked by a disulfide bond) in the gastrointestinal tract is more stable than the free amino acid cysteine. The disulfide bond is pepsin and trypsin-resistant, but may be split by heat, low pH, and mechanical stress. Cystine travels safely through the GI tract and blood plasma and is promptly reduced to the two cysteine molecules upon cell entry.



  • Cystine is the preferred form of cysteine for the synthesis of glutathione in macrophages and astrocytes. Lymphocytes and neurons prefer cysteine for glutathione production optimizing glutathione levels in macrophages and astrocytes with cystine allows these cells to provide cysteine to lymphocytes and neurons directly upon demand.

  • cystine

    Immunocal Bioactive Whey Protein is a specially prepared whey protein isolate which contains the thermolabile proteins serum albumin, alpha lactalbumin and lactoferrin. These proteins contain high levels of cystine residues that could be denatured by heat, low pH, or mechanical stress (inherent to most extraction processes). It is therefore recommended that high-speed mechanical blending or heating (above 118 degrees F) be avoided in the preparation of whey protein isolates such as Bioactive Whey Protein. In serum albumin there are 17 cystine residues and 6 glutamylcystine (Glu-Cys) dipeptides; in lactoferrin, 17 cystine residues and 4 GluCys dipeptides; and in alpha-lactalbumin, 4 cystine residues. In particular, the Glu-Cys dipeptides very readily enter the cell to be synthesized into GSH. Of interest, the Glu-Cys dipeptide is an exclusive feature of the only obligatory foods in the early life of mammals and oviparous species, those being milk and egg white respectively. When subject to heat or shearing forces, the fragile disulfide bonds within these peptides are broken and the bioavailability of the glutathione precursors is greatly diminished. As an antioxidant, glutathione is essential for allowing lymphocytes to express their full potential, without being hampered by oxyradical accumulation during the oxygen requiring development of the immune response. In a similar fashion, GSH delays the muscular fatigue induced by oxyradicals during the aerobic phase of strenuous muscular contraction. As a detoxification agent, glutathione has been demonstrated to be effective against a number of xenobiotics, including chemical pollutants, various carcinogens and ultraviolet radiation.

    Glutathione is a tightly regulated intracellular constituent and is limited in its production by negative feedback inhibition of its own synthesis through the enzyme gamma-glutamylcysteine synthetase, thus greatly minimizing any possibility of overdosage. [source: Physician's Desk Reference for Prescription Drugs (PDR) 2001, p. 1563].

  • Oral glutathione supplements as discussed previously, are virtually ineffective, since glutathione is a protein and is digested in the stomach before reaching the blood stream or tissues of the body. Researchers found that 3 grams of glutathione taken orally were ineffective in increasing circulating glutathione (glutathione in the bloodstream) in a clinical study evaluating the benefits of oral glutathione. Witschi A, Reddy S, Stofer B, Lauterburg BH. The systemic availability of oral glutathione. (source: Eur J Clin Pharmacol 1992;43(6):667-9) IV Glutathione is effective but expensive, uncomfortable, and somewhat impractical requiring infusions 2 times per week using an Intravenous (IV) line. Glutathione precursors are a better solution (except in acute cases of acetominophen overdose toxicity, where speed of administration is critical for hepatic preservation).


  • N-acetyl-L-cysteine (NAC) is an amine protected version of cysteine that is rapidly hydrolyzed in the body to the amino acid cysteine. (Cysteine is the monomer amino acid).

  • N-acetyl-L-cysteine

    NAC supplements are moderately effective, but dosing is limited due to toxic side effects (such as headache, dizziness, blurred vision) associated with cysteine supplementation.

    Cystine is a disulfide linked dimer of cysteine, and a rich nutritional source of cystine in the diet is undenatured whey proteins. The link is a disulfide bond which is readily reduced to the corresponding thiol (-SH).
    cystine

    Scientifically, the best way to increase glutathione levels is to take a supplement rich in cystine (a disulfide-bonded form of cysteine). Immunocal undenatured whey protein provides on of the richest sources of cystine known to science, and because cystine contains two weakly bonded molecules of cysteine, Immunocal is a unique "cysteine delivery vehicle".
    This form is virtually free of the toxic side effects associated with the single molecule (NAC). Two molecules of cysteine are connected by a weak disulfide bond to form a molecule of cystine. The disulfide-bonded cysteine is not digested, but is transported by the blood stream to the tissues of the body. Here, within the cells of the body, the weak disulfide bond between the two cysteine molecules is cleaved, and the cell has 2 molecules of cysteine from which glutathione can be manufactured. The greatest dietary source of cystine is bio-active, undenatured whey protein, and the only whey protein which has been studied in clinical trials at major Universities and Medical Schools and which is clinically proven to enhance or normalize glutathione levels is called "Immunocal". Bioactive Whey Protein is the only bioactive whey protein listed in the PDR (Physicians Desk Reference for Prescription Drugs), even though it is available without a prescription.
  • A good, certified, and inexpensive blood glutathione test is available for about $40. AMSCOT testing laboratories.
  • "A review article published in the Annals of Pharmacology stated that glutathione is important in DNA synthesis and repair, protein and prostaglandin synthesis, amino acid transport, detoxification of toxins and carcinogens, enhancement of the immune system, and protection from oxidation and enzyme activations." The Immune System Cure, Lorna R. Vanderhaeghe & Patrick J.D. Bouic, Ph.D.
  • Research suggests that abnormally low glutathione levels may increase your risk for Heart Attack. Eric Topol, MD, New England Journal of Medicine.
  • "Glutathione has potent anti-viral properties - if tissue and serum glutathione levels are significantly increased, the replication of most pathogens are slowed or stopped. Conversely, glutathione deficiency produces a pro-viral effect." Paul Cheney, M.D., Ph.D. and expert in the treatment of Chronic Fatigue Syndrome. Transcribed from a workshop presentation on the clinical management of Chronic Fatigue Syndrome
  • Lymphocytes, cells vital for effective immune function, depend on GSH for their proper function and replication.
    IMMUNOLOGY 61: 503-508 1987
  • As we age, there is a precipitous drop in GSH levels. Lower glutathione levels have been implicated in many diseases associated with aging.
    Journal of Clinical Epidemiology 47: 1021-28 1994
  • Antioxidants are well documented to play vital roles in health maintenance and disease prevention. GSH is your cells' own major antioxidant.
    Biochemical Pharmacology 47: 2113-2123 1994
  • GSH plays a role in eliminating many carcinogens as well as maintaining immune function.
    Cancer Letters 57: 91-94 1991
  • Strong muscular activity, such as that experienced by athletes, generates oxyradicals [free radicals] leading to muscle fatigue and poorer performance. GSH neutralizes these radicals.
    Sport Medicine 21: 213-238, 1996
  • GSH detoxifies many pollutants, carcinogens, and poisons, including many in fuel exhaust and cigarette smoke. It retards damage from radiation such as seen with loss of the ozone.
    Annual Reviews of Biochemistry 52: 711-780 1983


What is Glutathione (GSH)?

Glutathione, or GSH, is a naturally occurring protein that protects every cell, tissue, and organ from toxic free radicals and disease. It is a tripeptide of three amino acids - glycine, glutamate (glutamic acid), and cysteine. These precursors are necessary for the manufacture of glutathione within the cells.

Find Out More About Glutathione

PubMed is the U.S. National Library of Medicine's search service to access the 10 million citations in Medline and other related databases, with links to participating online journals published since 1966. When you access the PubMed site, enter your search word(s) into the form and click on the "Search" button. A list of abstracts will appear. Click on the author's name to read the abstract.

Narrow your search by entering "glutathione and [your health concern]" or you'll get over 107,000 abstracts on Glutathione!

Click on the "Advanced Search" button on the left menu bar to do a more refined search.

Use our simplified MEDLINE search page, or click on the link below to do your own advanced search.

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Scientific and Research information on Glutathione Enhancing whey proteins

23 published Immunocal clinical and scientific studies

The Clinical Management of Chronic Fatigue Syndrome (CFS, CFIDS) - transcript of a workshop by Paul Cheney, M.D., one of the leading authorities on Chronic Fatigue Syndrome and Fibromyalgia in the U.S., and founder/director of the Cheney Clinic, Feb. 1999. This study emphasized the central role of glutathione deficiency in the symptomology of Chronic Fatigue Syndrome.

CFS Radio Program - Feb. 28, 1999, Roger G. Mazlen M.D., Host, with Dr. Paul Cheney, discussing Dr. Cheney's CFS research.

The famous Louis Pasteur Institute for Research issues a book every year which goes to all the major medical schools in Europe, Canada, and the U.S.A. This book is entitled Oxidative Stress in Cancer, Aids and Neurodegenerative Diseases, co-authored by Luc Montagnier, co-discoverer of the AIDS virus. Chapter 42 of this book is entirely devoted to a discussion of Immune Enhancing Whey protein®. It reads, "Nutriceutical Modulation of Glutathione with a Humanized Native Milk Serum Protein Isolate, Bioactive Whey Protein: Application in Cancer and AIDS".

Montreal Children's Hospital: Dr. Larry Lands just presented results from a double-blind study in the area of Cystic Fibrosis and muscle performance in healthy young adults. He presented his findings at the American Lung Association's Symposium in San Diego, April 26th, 1999. Dr. Lands showed that Immune Enhancing Whey Protein® raised the cellular levels of glutathione in young athletes on the product by 35%, and improved muscle performance by up to 13%.

"Whey proteins in cancer prevention.", Bounous G, Batist G, Gold P Montreal General Hospital, McGill University, Quebec, Canada. "We and others have demonstrated that whey protein diets result in increased glutathione (GSH) concentration in a number of tissues, and that some of the beneficial effects of whey protein intake are abrogated by inhibition of GSH synthesis. Whey protein is particularly rich in substrates for GSH synthesis. We suggest that whey protein may be exerting its effect on carcinogenesis by enhancing GSH concentration."

    The Effect of Bioactive Whey Protein, Commercial Whey Protein, and Casein on Immune Response
    Bounous G, Batist G. Immunoenhancing property of dietary whey protein in mice:
    Role of glutathione. Clin Invest Med 12:154-61, 1989.
    Graph showing Optimization of the immune response in animals fed the Patented Whey Protein Concentrate (WPC)--Bioactive Whey Protein occured because of significantly greater glutathione production (>120%) in their lymphocytes (immune cells or white blood cells) than those animals fed Commercial WPC or Casein. This increased glutathione production following Bioactive Whey Protein supplementation was attributed to the abundance of known glutathione dietary precursors including serum albumin, alpha lactalbumin, and lactoferrin. Commercial whey protein contains significantly less of these precursors of glutathione. Additionally, the immunosustaining effect of Bioactive Whey Protein® Patented WPC was significantly greater than that of soy protein isolate in a study conducted by Bounous et al in Canada.

"The use of a whey protein concentrate in the treatment of patients with metastatic carcinoma: a phase I-II clinical study.", Kennedy RS, Konok GP, Bounous G, Baruchel S, Lee TD Department of Surgery, Dalhousie University, Halifax, Nova Scotia, Canada. "These results indicate that whey protein concentrate might deplete tumour cells of GSH and render them more vulnerable to chemotherapy."

    Graph showing results of Bioactive Whey Protein supplementation in mice and rats previously exposed to potent carcinogens (cancer-causing agents) resulted in a remarkably lower tumor mass than in those animals supplemented with casein, standard feed, or meat.
    Bounous G., et al. Clin Invest Med 11:213, 1988.
    This study was conducted with mice and rats exposed to (by feeding) potent carcinogens (cancer-causing agents). These animals were subsequently placed on protein diets of similar nutritional efficiency (Protein Efficiency Ratios, or PER), but from the three different protein sources. The COLON TUMOR MASS in animals fed the patented Whey Protein Concentrate (WPC) Bioactive Whey Protein was LOWER than the tumor mass in animals fed casein protein, standard feed, or meat, suggesting a protective effect associated with Bioactive Whey Protein supplementation. The immune stimulating effect of Bioactive Whey Protein Patented WPC was significantly greater than that of commercial Whey Protein Concentrate and Casein Protein in a separate study conducted by Bounous et al in Canada. Additionally, the immunosustaining effect of Bioactive Whey Protein Patented WPC was significantly greater than that of soy protein isolate in a study conducted by Bounous et al in Canada.

"Whey proteins as a food supplement in HIV-seropositive individuals.", Bounous G, Baruchel S, Falutz J, Gold P Department of Surgery, Montreal General Hospital, Quebec. "In conclusion, these preliminary data indicate that, in patients who maintain an adequate total caloric intake, the addition of "bioactive" whey protein concentrate as a significant portion of total protein intake increases body weight and shows elevation of glutathione (GSH) content of mononuclear cells toward normal levels."

"The biological activity of undenatured dietary whey proteins: role of glutathione." , Bounous G, Gold P Department of Surgery, Montreal General Hospital Research Institute, Quebec. "The presence in the serum albumin fraction of glutamylcysteine groups (rare in food protein) and the specific intramolecular bond as related to the undenatured conformation of the molecule are considered to be key factors in the glutathione-promoting activity of the protein mixture."

"The influence of dietary whey protein on tissue glutathione and the diseases of aging", Bounous G, Gervais F, Amer V, Batist G, Gold P Montreal General Hospital Research Institute, Quebec. "Hence a whey protein diet appears to enhance the liver and heart glutathione concentration in aging mice and to increase longevity over a 6.3 month observation period. "

"The immunoenhancing property of dietary whey protein concentrate.", Bounous G, Kongshavn PA, Gold P Montreal General Hospital Research Institute, Quebec, Canada."Mixing lactalbumin with either casein or soy protein in a 20 g protein/100 g diet formula significantly enhanced the immune response in comparison to that of mice fed diets containing 20% soy protein or casein."

"Immunoenhancing property of dietary whey protein in mice: role of glutathione.", Bounous G, Batist G, Gold P Montreal General Hospital, Quebec. "This is further evidence of the important role of glutathione in the immunoenhancing effect of dietary whey protein."

    Graph showing Superior Immunosustaining effect of Bioactive Whey Protein Patented WPC versus Casein and Isolated Soy Protein
    Bounous G. et al. J Nutr. 113:1415, 1983
    The immune response in animals fed the patented Whey Protein Concentrate (WPC) Bioactive Whey Protein was up to 400% greater than the immune response in animals fed casein or isolated soy proteins. Peak antibody production by speen lymphocytes (number of plaque forming cells) was measured after antigen challenge in mice fed protein diets of similar nutritional efficiency (Protein Efficiency Ratios, or PER), but from the three different protein sources. Similarly, the immune stimulating effect of Bioactive Whey Protein Patented WPC was significantly greater than that of commercial Whey Protein Concentrate in a separate study conducted by Bounous et al in Canada.

"Effect of supplementation with a cysteine donor on muscular performance." Lands LC, Grey VL, Smountas AA Division of Respiratory Medicine, McGill University Health Centre-Montreal Children's Hospital, Montreal, Quebec, Canada. "This is the first study to demonstrate that prolonged supplementation with a product designed to augment antioxidant defenses resulted in improved volitional performance. "

Longevity: A significant body of data is beginning to emerge suggesting a benefit of glutathione enhancement in longevity. Several animal studies have demonstrated a 35% to 50% increase in longevity as compared to matched controls. In addition to living longer, these animals were healthier and had fewer degenerative conditions.


For CLINICAL AND SCIENTIFIC REFERENCES used in this article, please click HERE.
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