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WPI-90S With Organic Selenium

Dietary Nutrition SupplementsNatural Biological AlternativesGSH Glutathione Cysteine/Cystine


Description WPI-90S: Our New agglomerated micro filtered pure whey protein isolate with organic selenium (selenomethionine) nutritional food, is of the highest quality and purity, using a new patent pending low temperature process, to preserve the biological nature and activity of the product.

WPI-90S should be taken 1/2 to 1 hour before meals at a rate of 10 grams / 1 to 2 times per day

Note: Nutritecks products are fine grind soluble concentrated ready to use powders, which may be mixed or added to warm water (not hot) yogurt and most of your regular non alcoholic beverages or simply sprinkled on cereals  (like sprinkling spices), without compromising product effectiveness or quality. Keep containers closed in a cool dry area to prevent contamination before/after use.

Health Canada Our Product License Number NPN : 80025325


Packaging: 300 grams
Serving Size: 10 grams   Servings per container: 30 / 30 day supply


     Amount per Serving

        % Daily Value †





    9.20 g

      0.0 g

      0.2 g

     175 mcg




RDI.. 100.0%

Ingredients: Whey protein isolate soluble agglomerated and micro-filtered with organic selenium - selenomethionine

* Daily Value not established / % daily values are based on a 2,000-calorie diet.

Suggested Use: As a food supplement take a 10 gram scoop (included) with water or juice daily, before meals, or as directed by your health care professional.

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Description: High Nutritional Value, Low Lactose, Low Fat.

Packaging: 300 gram jars / 30 day supply

Note: Nutritecks products are fine grind concentrated ready to use powders, which may be mixed or added to water and most of your regular non alcoholic beverages or simply sprinkled on your foods (like sprinkling spices), or may even be packaged in standard pill and capsule serving methods without compromising product effectiveness or quality.

Please Note: When calculating your costs of similar products in capsule or pill form which are normally packaged in Example: 4 x 250 mg = 1 gram or 1000 mg. Our 225 gram container has the equivalent of 1000 x 225 mg pills or capsules which results in very considerable savings of from 50 to 70% of the cost in many cases of pill and capsule packaging. 

Bulk Powder Packaging: 225 grams Price: $48.70 - Free Shipping - USA Canada

Wholesale prices are now available for health care practitioners, natural food stores, dealers and distributors.

Minimum order is 12 units plus for wholesale pricing - Please contact us E-mail for further details.  

 Toll Free Order Desk: USA & Canada : 1-888-205-9957 

 Educational Research References


Glutathione and its dependent enzymes play an important role in defense mechanisms that protect against cancer. The provision of glutathione precursors by whey proteins may explain the ability of dietary whey proteins to enhance both humoral and cell-mediated immune responses in laboratory animals. Whey contains growth factors with anti-cancer action at extremely low concentrations, and these compounds may survive digestion in sufficient quantities to generate a physiological response. Whey protein concentrate also contains the membrane phospholipid sphingomyelin, which has a strong ability to suppress tumor growth.

These proteins contain exceptional amounts of cysteine (cys-cys) and glutamyl cysteine (glu-cys) (Somersall, and Bounous, 1999). Meister, 1983, demonstrated that the Glu-Cys precursors of GSH can easily enter the cell and therefore be synthesized into GSH. It thus becomes noteworthy that the most labile milk proteins - Serum Albumin and Lactoferrin - are those which contain these putative GSH-promoting peptide components (Baruchel et al, 1996). Interestingly, the Glu-Cys di-pepetide is an exclusive feature of the only obligatory foods in the early life of mammals and oviparous species, i.e. Milk and egg white respectively (Bounous and Gold, 1991)

When undenatured, lactoferrin, serum albumin and Alpha lactalbumin contain almost the same number of cystine residues per total amino acid (Eigel et al, 1984; Goodman and Schanbacher, 1991). Hence, in serum albumin, there are 17 cystine residues per 66,000 MW molecule, and six Glu-Cys dipeptides (Eigel et al, 1984); in Lactoferrin 17 cystine residues per 77,000 MW, and four Glu-Cys dipeptides (Goodman and Schanbacher, 1991); and in Alpha-Lactalbumin, four cystine residues per 14,000 MW molecule (Eigel et al, 1984). On the other hand beta-lactoglobulin has only two cystine residues per 18,400 MW molecule (Eigel et al, 1984), and IgG1, the predominant immunoglobulin in cows milk serum, only four disulfide bridges (cystine) per 166,000MW molecule (Baruchel et al, 1996).

Undenatured whey proteins and more specifically, the cystine rich thermolabile proteins, represent an effective cysteine delivery system for the cellular synthesis of glutathione. Cellular GSH depletion has been implicated in the pathogenesis of a number of degenerative conditions and disease states including Parkinson's, Alzheimer's, arteriosclerosis, cataracts, cystic fibrosis, malnutrition, aging, AIDS, and cancer (Bounous and Gold, 1991). When GSH's metabolic functions are considered as a whole, it is easy to see how cellular GSH deficiency compromises health, performance and quality of life. Some of GSH's metabolic functions are as follows: enhancement of immune function, elimination of toxins, elimination of carcinogens, antioxidant cell protection, protection against ionizing radiation, DNA Synthesis and repair, protein synthesis, prostaglandin synthesis, Leukotriene synthesis, amino acid transport, enzyme activation and regulation (Gutman and Schettini, 1998).

Whey protein isolate can provide those essential building blocks which are essential to GSH formation. It has been recently reported by Land et al, 1999 that augmenting the availability of cysteine may positively affect immune function. According to Dröege and Holm, 1997 conditions that are associated with low cystine and glutamine concentrations also demonstrate decreased natural killer cell activity. GSH plays a central role in the functioning of immune cells, in particular it's creation and maintenance of T-cell lymphocytes, the body's frontline defense against infection (Gutman and Schettini, 1998). Bounous et al, 1993, reported that a proprietary WPI has potential therapeutic benefits in conditions leading to immunodeficiency. It was observed by these researchers that the humoral immune response of mice fed the proprietary WPI diet was almost five times greater than the corresponding values for mice fed a casein diet and a cysteine enriched casein diet.

Augmented GSH production under conditions of homeostatic challenge will place demands upon available cysteine resources. Lymphocyte GSH levels and immune responsiveness can be influenced by feeding the rate limiting precursor of GSH, Bounous et al., 1989. Their studies show that the administration of cysteine in the form of a proprietary WPI mixture was far more effective than when administering the rate limiting precursor of GSH as free cysteine. Fidelus and Tsan, 1986, showed that modulation of intracellular glutathione may indeed affect immune responsiveness.

By maintaining high intracellular GSH levels, oxidative damage is minimized (Fidelus and Tsan, 1986; Gougerot-Pocidalo et al, 1988). In fact the capacity of a cell to recover from an oxidative insult is considered to be represented by its ability to regenerate intracellular stores of Glutathione (Noelle and Lawrence, 1981) This can also prevent disease or aid recovery. Even when an animal does not come down with an illness, it's immune system will be primed to fight it. In this way one can take advantage of both approaches to health, prevention and therapeutic.

The mechanisms responsible for depletion of glutathione levels are varied and often times need to be corrected prior to establishing pre-depletion levels of glutathione or ultimately, optimum levels. Nutritional deprivation has a major effect on an animal's ability to maintain, and/or increase glutathione. For example, the biosynthetic supply of reduced glutathione is sufficient to withstand an inflammatory challenge in well-nourished animals but not in protein deficient or amino acid imbalanced animals. Also, the amount of free radical exposure or reactive oxygen derive molecules has a significant effect on how quickly glutathione levels can be replenished. The availability of cystine within the cell is the apparent rate limiting factor in the synthesis of glutathione to replenish the cell's store during the immune response or after oxidative molecule challenge.

Given the nature of the active peptides, or "bioactive peptides", in whey protein, the oral administration of these peptides induces a rapid replenishment of glutathione (GSH) especially in the lymphocyte during the GSH-depleting development of the immune response. It is likely that immunoactive di-and tri- peptides can pass freely across the intestinal wall and react directly with peripheral lymphocytes. The amount of cellular (GSH) is a tightly self-regulated system because of the feedback inhibition of gamma-glutamylcystine synthetase activity by the GSH level (Richman and Meister, 1975). In reality, the Cystine delivery system of whey protein produces a substantial increase in cellular GSH up to but not above normal values.

Whey protein releases Cystine or glutamylcystine in the small intestine and after transport in the blood plasma, these Cystine di-peptides effectively cross the cell's membrane. Cystine di-peptides remain stable in the circulation, unlike glutathione itself.

It is well accepted that the absorption of di- and tri- peptides from the gastrointestinal tract is an important biological phenomenon and a significant proportion of circulating amino acids are in the form of small peptides (Power and Murphy, 1999). Once liberated in the body, bioactive peptides perform an impressive array of regulatory functions and display a wide range of other activities.

The bioactivity of whey protein is dependant upon a criticalconcentration of various bioactive proteins one of which being Lactoferrin. Several antimicrobial peptides can be derived from the protein Lactoferrin. Lactoferrin is a well-characterized iron-binding glycoprotein that occurs in mammalian body fluids, most notably milk. As an intact protein, its is considered to be an important host defense against microbial infections. Enzymatic cleavage of Lactoferrin has been demonstrated to produce three distinct peptides with antibacterial activity towards entertoxigenic E. coli. Two of these peptides display antimicrobial activity toward a number of pathogenic microorganisms, while a third peptide has been reported to inhibit the growth of Listeria monocytogenes. (Power and Murphy, 1999)

The innate structure and composition of whey protein enable its bioactive proteins rapid and efficient absorption. The presence of milk derived peptides enables one to make scientifically viable conclusions. It is a well-known fact that part of the importance of dietary protein is manifested through intermediate biologically active peptides formed as a part of the degradation process in the gastrointestinal tract. Significant evidence may be found in the literature to support the notion of nutritionally important, bioactive peptides over free amino acids and intact protein have been reported in the literature (Siemensma et al., 1993).

These include: Transport of short peptides across the intestinal wall is facilitated compared to free amino acids.

Peptides are less hypertonic than free amino acids and this has the net effect of increasing their efficiency of absorption and reduces osmotic problems.

Short peptides, in many cases, are less antigenic than larger polypeptides or the native protein from which they are derived.

There is evidence from animal and cell culture studies that milk proteins have anti-carcinogenic properties. This review discusses the anti-carcinogenic potential of milk proteins provided by whey protein isolate. Proteins supplying the sulfur amino acids cysteine and methionine appear to play a central role in tumor prevention. Milk components such as bovine serum albumin, alpha-lactalbumin and lactoferrin are also rich sources of gamma-glutamylcysteine, which can be utilized at the cellular level to synthesize glutathione. Australian Journal of Dairy Technology 1998, 53:37-47

Selenomethionine is well absorbed and retained. From selenomethionine, all other needed selenium compounds are produced in the body. On the other hand, selenomethionine, like its sulfur analog, methionine, cannot be synthesized efficiently in the human organism. All quality nutritional selenium supplements should therefore contain selenomethionine

Selenium is an essential mineral in human nutrition. Selenium Yeast is a natural dietary selenium supplement with clinically proven physiological value in improving the selenium status in man. Selenium is a known anti oxidant and is an essential component of Glutathione peroxidase enzyme, which inactivates tree radicals.

Selenium is required in thyroid metabolism while converting active thyroid hormone (14) into the inactive thyroid hormone (13). lnactivates heavy metals, especially mercury, lead and cadmium.

Borglund, M and Akesson, B. 1988 Effect of selenium supplementation on the distribution of selenium in plasma proteins of health subjects. lnternat. J. Vit. Nutr. Res. 58, 97-102.

Clark, L C. et. al., 1996 Effects of selenium supplementation cancer prevention in patients with carcinoma of the skin. iouri American Medical Assoc. 276 (24), 1957-1963.

Clausen, J. and Nielsen, S. A. 1998 Comparison of whole blood se nium values and erythrocytes of glutathione peroxidase activities normal individuals on supplementation with selenate, seleni L-selenomethionine and high selenium yeast. Biol. Trace EIem. R15, 125-138.

Kumpulainen, i., Salmenpera, L, Siimes, M.A., Koivistoinen, P., a Perheentupa, i. 1985 Selenium status of exclusively breast-I infants as influences by maternal organic or inorganic selenium si plementation. i. Amer. Clin. Nutr. 42, 829-835.



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