this product is listed in the U.S. Physicians' 2001 PDR
(Physicians Desk Reference) & Doctors Redbook.

PDR® entry for glutathione Powder Sachets (This Company )

DESCRIPTION

THI PRODUCT is a U.S. patented natural food protein concentrate which assists the body in maintaining an optimal concentration of glutathione (GSH) by supplying the precursors required for intracellular glutathione synthesis. These precursors are derived from a specially prepared bovine whey protein isolate. Glutathione (L-gamma-glutamyl-L-cysteinylglycine) 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.

CLINICAL PHARMACOLOGY

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 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 biochemical activity of glutathione. 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. this product can thus be viewed as a cystine delivery vehicle.

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 allow these cells to provide cysteine to lymphocytes and neurons directly upon demand.

This specially prepared whey protein isolate 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 in most extraction processes). In serum albumin there are 17 cystine residues and 6 glutamylcystine (Glu-Cys) dipeptides; in lactoferrin 17 cystine residues and 4 Glu-Cys 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.

INDICATIONS AND USAGE

this productis a natural food supplement and as such is limited from stating medical claims per se. Statements have not been evaluated by the FDA. As such, this product is not intended to diagnose, cure, prevent or treat any disease.

Glutathione augmentation is a strategy developed to address states of glutathione deficiency, high oxidative stress, and xenobiotic overload in which glutathione plays a part in the detoxification of the xenobiotic in question. Glutathione deficiency states include, but are not limited to: AIDS and cancer cachexia, chemical and infectious hepatitis, radiation poisoning, malnutritive states, arduous physical stress, and has been associated with sub-optimal immune response. Many clinical pathologies are associated with oxidative stress and are elaborated upon in numerous medical references.

CONTRAINDICATIONS

this productis contraindicated in individuals who develop or have known hypersensitivity to specific milk proteins.

PRECAUTIONS

Each sachet of this product contains nine grams of protein. Patients on a protein-restricted diet need to take this into account when calculating their daily protein load. Although a bovine milk derivative, this product contains less than 1% lactose and therefore is generally well tolerated by lactose-intolerant individuals.

WARNINGS

Patients undergoing immunosuppressive therapy should discuss the use of this product with their health professional.

Heating or adding this product to a hot liquid, or use of a high-speed blender to reconstitute it will significantly decrease the effectiveness of the product.

ADVERSE REACTIONS

Gastrointestinal bloating and cramps if not sufficiently rehydrated. Transient urticarial-like rash in rare individuals undergoing severe detoxification reaction. Rash abates when product intake stopped or reduced.

OVERDOSAGE

Overdosing on this product has not been reported. Unless hypersensitive to the constituents, no toxicity of milk proteins has been described.

DOSAGE AND ADMINISTRATION

Maintenance dose is one sachet (10 grams) per day. For mild to moderate health challenges, higher doses are recommended. Clinical trials in patients with AIDS, cancer and chronic fatigue syndrome have used 30-50 grams per day without ill effect. this product is best administered on an empty stomach or with a light meal. Concomitant intake of another high protein load may adversely affect absorption.

RECONSTITUTION: this product is a dehydrated powdered protein isolate. It must be appropriately rehydrated before use. If left standing too long after rehydration, activity of the product may be reduced. Times vary depending on temperature and pH of the liquid used. It is generally recommended to ingest the product within 30 minutes of reconstitution. DO NOT heat or use a hot liquid to rehydrate the product or use a high-speed blender for reconstitution. These methods will decrease the activity of the product. Special low-speed blenders or mixing cups can be made available through NuMedTec distribution networks.

Proper mixing is imperative. Consult instructions included in packaging.

HOW SUPPLIED

10 grams of bovine milk protein isolate powder per sachet.

30 sachets per box.

STORAGE

Store in a cool dry environment. Refrigeration is not necessary.

Patent no.'s 5,230,902 - 5,290,571 - 5,456,924 - 5,451,412 - 5,888,552

REFERENCES

1. Meister A. Glutathione. Ann Rev Biochem 52:711-60, 1983.
2. Kaplowitz N, Aw T, Ookhtens M. The regulation of hepatic glutathione. Ann Rev Pharmacol Toxicol 25:715-44, 1985.
3. Witschi A, Reddy S, Stofer B, Lauterberg B. The systemic availability of oral glutathione. Eur J Clin Pharmacol 43:667-9, 1992.
4. Meister A. New aspects of glutathione biochemistry and transport, selective alteration of glutathione metabolism. Nutr Rev 42:397-410, 1984.
5. Bray T, Taylor C. Enhancement of tissue glutathione for antioxidant and immune functions in malnutrition. Biochem Pharmacol 47:2113-23, 1994.
6. Lomaestro B, Malone M. Glutathione in health and disease: Pharmacotherapeutic Issues. Ann Pharmacother 29:1263-73, 1995.
7. Bounous G, Gold P. The biological activity of undenatured whey proteins: The role of glutathione. Clin Invest Med 14:296-309, 1991.
8. Bounous G, Kongshavn P. Influence of dietary whey proteins on the immune system of mice. J Nutr 112:1747-55, 1982.
9. Bounous G, Letourneau L, Kongshavn P. Influence of dietary protein type on the immune system of mice. J Nutr 113:1415-21, 1983.
10. Bounous G, Kongshavn P. Influence of protein type in nutritionally adequate diets on the development of immunity. Absorption and utilization of amino acids 2:219-32, 1989.
11. Bounous G, Batist G, Gold P. Immuno-enhancing property of dietary whey protein in mice: Role of glutathione. Clin Invest Med 12:154-61, 1989.
12. Bounous G, Shenouda N, Kongshavn P, Osmond D. Mechanism of altered B-cell response induced by changes in dietary protein type in mice. J Nutr 115:1409-17, 1985.
13. Bounous G, Papenburg R, Kongshavn P, Gold P, et al. Dietary whey protein inhibits the development of DMH-induced malignancy. Clin Invest Med. 11:213-17, 1988.
14. Bounous G, Gervais F, Amer V, Batist G, et al. The influence of dietary whey protein on tissue glutathione and the diseases of aging. Clin Invest Med 12:343-9, 1989.
15. Baruchel S, Viau G, Olivier R, Bounous G, Wainberg MA. Nutriceutical modulation of glutathione with a humanized native milk serum protein isolate this product: Application in AIDS and cancer. In: Oxidative stress in Cancer AIDS and Neurodegenerative Diseases. Ed.; Montagnier L, Olivier R, Pasquier C. Pub.; Marcel Dekker Inc. New York, 1996.
16. Kennedy R, Konok G, Bounous G, Baruchel S, Lee T. The use of a whey protein concentrate in the treatment of patients with metastatic carcinoma: A phase I-II clinical study. Anticancer Research 15:2643-50, 1995.
17. Baruchel S, Bounous G, Gold P. Place for an antioxidant therapy in HIV infection. Oxidative stress, Cell activation and viral infection , 311-21,1994.
18. Bounous G, Baruchel S, Falutz J, Gold P. Whey proteins as a food supplement in HIV-seropositive individuals. Clin Invest Med. 16:3; 204-209.
19. Baruchel S, Viau G. In-vitro selective modulation of cellular glutathione by a humanized native milk protein isolate in normal cells and rat mammary carcinoma mode. Anticancer Research. 16:1095-1100, 1996.
20. Bounous G, Batist G, Gold P. Whey proteins in cancer prevention. Cancer Letters. 57:91-94, 1991.
21. Watanabe A, Higuchi K, Yasumura S, Shimizu Y, Kondo Y, Kohri H. Nutritional modulation of glutathione level and cellular immunity in chronic hepatitis B and C. Hepatology. 24:597A, 1996.
22. Lothian B, Grey V, Kimoff RJ, Lands LC. Treatment of obstructive airway disease with a cysteine donor protein supplement: A case report. Chest 117:914-916, 2000.
23. Cross CE, Halliwell B, Borish ET, et al. Oxygen radicals and human disease. Annals of Internal Medicine 107:526-545, 1987.
24. Lands LC, Grey VL, Smountas AA. Effect of supplementation with a cysteine donor on muscular performance. J. Appl. Physiol. 87:1381-1385, 1999.
25. Short S, Merkel BJ, Caffrey R, McCoy KL. Defective antigen processing correlates with a low level of intracellular glutathione. Eur. J. Immunol. 26(12):3015-3020, 1996.
26. Macho A, Hirsch T, Marzo I, Marchetti P, Dallaporta B, Susin SA, Zamzami N, Kroemer G. Glutathione depletion is an early and calcium elevation is a late event of thymocyte apoptosis. J. Immunol. 158(10):4612-4619, 1997.
27. Gmunder H, Eck HP, Benninghoff B, Roth S, Droge W. Macrophages regulate intracellular glutathione levels of lymphocytes. Evidence for an immunoregulatory role of cysteine. Cell. Immunol. 129(1)32-46, 1990.
28. Kranich O, Dringen R, Sandberg M, Hamprecht B. Utilization of cysteine and cysteine precursors for the synthesis of glutathione in astroglial cultures: preference for cystine. Glia 22(1):11-18, 1998.
29. Droge W, Holm E. Role of cysteine and glutathione in HIV infection and other diseases associated with muscle wasting and immunological dysfunction. FASEB J. 11(13):1077-1089, 1997.

This Company 's

http://www.immunotec.biz/bestwhey4health/

---

More...

---

Download this Free Report

Get a FREE personalised website and
40% off the price when you
Become an Entrepreneur Today