Original article
We get questions everyday from people that have questions about protein and how it effects performance and endurance. Most people are rightfully confused because of overwhelming amount of inaccurate information that’s available. We’ve assembled this overview to explain the basic differences in whey proteins. If you have a question that’s not addressed, post it in the blog and we’ll make sure you get the information you’re looking for.
Whey Protein
Whey protein is a high quality complete protein containing all of the
essential amino acids required by the body each and every day. There
are several different methods that are used today evaluate protein
quality. No matter which method is used, whey proteins have been proven
to be an excellent, pure source of protein.
Whey Protein References
Hoerr R.A., Bostwick E.F., 2000. “Bioactive proteins and probiotic bacteria: modulators of nutritional health.” Nutrition, July-August, 16(7-8): 711-713
Boirie, Y., et al., 1997. “Slow and fast dietary proteins differently modulate post-prandial protein accretion.” Proceedings of the National Academy of Sciences, 94:14930-14935.
Dangin, M., Boirie, Y., Guillet, C., and Beaufrere, B. 2002. “Influence of the protein digestion rate on protein turnover in young and elderly subjects.” Journal of Nutrition, October, 132:3228S-3233S.y of Sciences, 94:14930-14935.
Tolia, V., Lin, C., and Kuhns, L. 1992. “Gastric emptying using three different formulas in infants with gastroesophaegeal reflux.” Journal of Pediatric Gastroenterology and Nutrition, 15(3):297-301.
Appel, L. et. al., 1997. “A clinical trial of the effects of dietary patterns on blood pressure.” The New England Journal of Medicine, 336(16):1117-1124.
FitzGerald, R.J., Meisel, H., 1999. “Lactokinins: Whey protein-derived ACE inhibitory peptides.” Nahrung 43:165-167.
FitzGerald, R.J., Meisel, H., 2000. “Milk protein-derived peptide inhibitors of angiotensin -1-converting enzyme.” British Journal of Nutrition. 84:S33-S37.
Groziak S.M, Miller G.D., 2000. “Natural bioactive substances in milk and colostrum: effects on the arterial blood pressure system.” British Journal of Nutrition, Supplement, November, 84(1):S119-S125.
Esmarck, J.L., Andersen, Olsen, S., Richter, E.A., Mizuno, M., and Kjaer, M., 2001, “Timing of postexercise protein intake is important for muscle hypertrophy with resistance training in elderly humans.” Journal of Physiology, 535.1:301-311.
McCarron, D.A., 1998. “Diet and high blood pressure – the paradigm shift.” Science, 281:933.
McCarron, D. A., 2000. “Dietary calcium and blood pressure control: lessons learned from controlled clinical trials.” Bulletin of the International Dairy Federation, 353:6-9.
Miller, G.D. et al., 2000. “Benefits of dairy product consumption on blood pressure in humans: a summary of the biomedical literature.” Journal of the American College of Nutrition, April 19 (2 Suppl): S147-S164.
Mullally, M., Meisel, H. and Fitzgerald, R., 1997. “Angiotensin-I-Converting enzyme inhibitory activities of gastric and pancreatic proteinase digests of whey proteins.” International Dairy Journal, 7:299-303.
Pfeuffer, M., Schrezenmeir, J., 2000. “Bioactive substances in milk with properties decreasing risk of cardiovascular diseases.” British Journal of Nutrition, Supplement, 84(1):S155-S159.
Pihlanto-Leppala, A. et.al., 2000. “Angiotensin I-converting enzyme inhibitory properties of whey protein digest: concentration and characterization of active peptides.” Journal of Dairy Research, 67:53-64.
Pins, J., and Keenan, J., 2002. “The antihypertensive effects of a hydrolyzed whey protein isolate supplement (BioZate 1®).” Cardiovascular Drugs and Therapy, 16(Supp. 1):68.
Rutherford, K. J., Gill, H.S., 2000. “Peptides affecting coagulation.” British Journal of Nutrition, 84:S99-S102.
Sharpe, S.J., Gamble, G.D., Sharpe, D.N., 1994. “Cholesterol-lowering and blood pressure effect of immune milk.” American Journal of Clinical Nutrition, 59:929-934.
Bounous, G., 2000. “Whey protein concentrate (WPC) and glutathione modulation in cancer treatment.” Anticancer Research, 20:4785-4792.
Bounous, G., Baptist, G., and Gold, P., 1991. “Whey proteins in cancer prevention.” Cancer Letters 57:91. Hakkak, R., Korourian, S., Shelnutt, S. R., et. al., 2000. “Diets containing whey proteins or soy protein isolate protect against 7,12-Dimethylbenz (a) anthracene-induced mammary tumors in female rats.” Cancer Epidemiology, Biomarkers & Prevention, 9:113-117.
Hakkak, R., Korourian, S., Ronis, M.J., Johnston, J., and Badger, T., 2001. “Dietary whey protein protects against azoxymethand-induced colon tumors in male rats.” Cancer Epidemiology, Biomarkers & Prevention, 10:555-558.
Kennedy, R. et. al., 1995. “The use of a whey protein concentrate in the treatment of patients with metastatic carcinoma: A phase I-II clinical study.” Anticancer Research, 15:2643-2650.
McIntosh, G.H., et al., 1995. “Dietary proteins protect against dimethylhydrazine-induced intestinal cancers in rats.” Journal of Nutrition, 125:809-816.
Takada, Y., Aoe, S., Kumegawa, M., 1996. “Whey protein stimulates the proliferation and differentiation of osteoblastic MC3T3-E1 Cells.” Biochemical and Biophysical Research Communications, 223:445-449.
Tsai, W., Chang, W., Chen, C.H., and Lu, F., 2000. “Enhancing effect of patented whey protein isolate (Immunocal) on the cytotoxicity of anti-cancer drug.” Nutrition and Cancer, 38(2):200-208.
Tsuda, H., et al, 2000. “Milk and dairy products in cancer prevention: focus on bovine lactoferrin.” Mutation Research, 462:227-233.
Bounous, G., Gervais, F., Amer, V., Batist, G., Gold, P., 1989. “The influence of dietary protein on tissue glutathione and the diseases of aging.” Clinical Investigative Medicine, 12, 6:343.
Bounous, G, Gold, P., 1991. “The biological activity of undenatured dietary whey proteins: role of glutathione.” Clinical Investigative Medicine, 14(4):296-309.
Bounous, G. et. al., 1989. “Immunoenhancing property of dietary whey protein in mice: role of glutathione.” Clinical Investigative Medicine, 12:154-161.
Bounous, G., Molson, J., 1999. “Competition for glutathione precursors between the immune system and the skeletal muscle: Pathogenesis of chronic fatigue syndrome.” Medical Hypothesis, 53(4):347-349.
Docena, G.H. et. al., 1996. “Identification of casein as the major allergenic and antigenic protein in cow’s milk.” Allergy, 51(6):412-416.
Kennedy, R.S., Bounous, G., Konok, G.P., Baruchel, S., Lee, T.D.G., 1995. “The use of a whey protein concentrate in the treatment of patients with metastatic carcinoma: A phase I-II Clinical Study.” Anticancer Research, 15:2643-2650.
Kuwata, H. et.al., 1998. “Direct evidence of the generation in human stomach of anti-microbial peptide domain(lactoferricin) from ingested lactoferrin.” Biochem. Biophys Acta, 1429:129-141.
LeBoucher, J. et al., 1999. “Modulation of immune response with ornithine A-ketoglutarate in burn injury: an arginine or glutamine dependency?” Nutrition, October, 15(10):773-777.
Wang, H., Ye, X., Ng, T.B., 2000. “First demonstration of an inhibitory activity of milk proteins against human immunodeficiency virus-1 reverse transcriptase and the effect of succinylation.” Life Sciences, 67:2745-2752.
Wong, C.W. et al., 1997. “Effects of purified bovine whey factors on cellular immune functions in ruminants.” Veterinary Immunology and Immunopathology, 56:85-96.
Lemon, W.R. et al, 1996. “Is increased dietary protein necessary or beneficial for individuals with a physically active lifestyle?” Nutrition Reviews Supplement, 54:S169-175.
Lemon, W.R., 1998. “Effects of exercise on dietary protein requirements.” International Journal of Sport Nutrition and Exercise Metabolism, 8(4): 426-447.
Beeh, M., Schlaak, J.F., Buhl, R., 2001. “Oral supplementation with whey proteins increases plasma glutathione levels of HIV infected patients.” European Journal of Clinical Investigation, February, 31 (2):171-178.
Berkhout, B. et al., 2002. “Characterization of the anti-HIV effects of native lactoferrin and other milk proteins and protein-derived peptides.” Antiviral Research, 55:341-355.
Bounous, G. et. al., 1991. “Whey protein as a food supplement in HIV-seropositive individuals.” Clinical Investigative Medicine, 16(3):204-209.
We get questions everyday from people that have questions about protein and how it effects performance and endurance. Most people are rightfully confused because of overwhelming amount of inaccurate information that’s available. We’ve assembled this overview to explain the basic differences in whey proteins. If you have a question that’s not addressed, post it in the blog and we’ll make sure you get the information you’re looking for.
Whey Protein
Whey protein is a high quality complete protein containing all of the
essential amino acids required by the body each and every day. There
are several different methods that are used today evaluate protein
quality. No matter which method is used, whey proteins have been proven
to be an excellent, pure source of protein.
To help prevent the breakdown of muscle tissues, whey protein
contains beta-lactoglobulin, a rich source of branched-chain amino
acids (BCAAs). Whey protein is also a rich source of the amino acid
Cystein and has been shown to increase glutathione levels in the body.
Glutathione is an antioxidant that helps provide an added boost to the
immune system.
Whey proteins have a Protein Digestibility Corrected Amino Acid Score (PDCAAS)
of 1.14. The reported score is 1.0, which is the maximum value allowed
by the USDA for reporting purposes. The PDCAAS is the USDA’s officially
approved method of scoring protein quality.
Another method used to measure protein quality is the Protein Efficiency Ratio (PER). Whey proteins have a PER of 3.2, making it one of the highest single source proteins. The PER rating is based upon the evaluation of the growth of animals consuming a fixed amount of dietary protein from a single source. As the PER increases, so does the quality of the protein.
Biological Value (BV), another measure of protein quality, measures the amount of protein that is retained from the absorbed protein for maintenance and growth. It measures the fraction of the nitrogen in the diet that remains after the nitrogen losses in the waste products have been subtracted. Whey proteins have a biological value of 100, which is higher than the value for casein (milk protein), soy protein, beef, or wheat gluten
Whey protein is not a single protein; it consists of a number of
individual protein components. In recent years new technology has
enabled manufacturers to isolate and further purify some of these
individual components, including technology that allows the protein to
be isolated from the fats and sugars (whey isolate or hydrolysate). Due
to its lower molecular weight, whey in its isolate form is more quickly
and fully absorbed than other forms. The following is a list of the
individual components in whey protein:
Another method used to measure protein quality is the Protein Efficiency Ratio (PER). Whey proteins have a PER of 3.2, making it one of the highest single source proteins. The PER rating is based upon the evaluation of the growth of animals consuming a fixed amount of dietary protein from a single source. As the PER increases, so does the quality of the protein.
Biological Value (BV), another measure of protein quality, measures the amount of protein that is retained from the absorbed protein for maintenance and growth. It measures the fraction of the nitrogen in the diet that remains after the nitrogen losses in the waste products have been subtracted. Whey proteins have a biological value of 100, which is higher than the value for casein (milk protein), soy protein, beef, or wheat gluten
- Beta Lactoglobulin: The most abundant whey protein component, making up approximately 50-55% of the whey protein. Binds fat soluble vitamins making them more available to the body. Provides an excellent source of essential and branched chain amino acids (BCAAs), which help prevent muscle breakdown and spare glycogen during exercise. Hydrolyzed versions are often used in infant formulas to reduce potential allergic reactions.
- Alpha-lactalbumin: The second most abundant whey protein component, making up approximately 20-25% of the whey protein. The primary protein found in human breast milk. High in tryptophan, an essential amino acid; potential benefits include sleep regulation and mood improvement under stress. Excellent source of essential amino acids and BCAAs. The only whey protein component capable of binding calcium.
- Immunoglobulins: Makes up approximately 10-15% of the whey protein. Provides immunity enhancing benefits to infants and others. Predominant whey protein component found in colostrum.
- Bovine Serum Albumin: Makes up approximately 5-10% of the whey protein. Large sized protein with a good essential amino acid profile and fat binding properties.
- Lactoferrin: Makes up approximately 1-2% of the whey protein. Inhibits the growth of bacteria (including some pathogenic bacteria) and fungi due to its ability to bind iron. Iron is an essential nutrient often required for bacterial growth. The USDA recently approved the use of lactoferrin on meat to prevent the growth of pathogens such as E. coli and Salmonella. Promotes the growth of beneficial bacteria such as Bifidus. Helps infants establish good microbial conditions in the intestines. Regulates iron absorption and bio-availability. May help to reduce inflammation. An antioxidant that naturally occurs in many body secretions such as tears, blood, breast milk, saliva and mucus.
- Lysozyme Makes up less than 0.1% of the whey protein. Contains immunity enhancing properties.
Whey Protein Isolate
Whey protein isolate is the purest form of whey protein and contains
90-95% protein. It contains little, if any, fat or lactose. In contrast,
whey protein concentrate can have a protein content ranging from 25%
to 89%. It will contain some lactose, fat, and minerals. As the protein
level increases the amount of lactose decreases. Whey protein
concentrate at 70% – 80% protein content is the form most readily
available as a protein powder supplement.7
Whey protein, a milk derivative, is by far the most popular protein on the market and comes in various forms, from the lower grade, higher fat whey concentrate to the highly purified isolate or hydrolysate form (the latter of which provides the benefits of microfractions and is low in fat and lactose). Most of the whey protein on the market is usually found as ion-exchange, a process using electric charges to extract the protein. There are some advanced procedures (like cross flow microfiltration) that produce higher quality whey, with subsequent added benefits over ion-exchange whey isolate in preserving key microfractions which are essential to its benefits. Whey protein isolate that is not heat-treated contains key microfractions, like alpha lactalbumin and glycomacropeptides, which can both positively support immune function. Some of the microfractions or growth factors found in whey protein can even enhance IGF-1 levels which can increase lean muscle mass—good news for hard training athletes. Whey protein has a very high biological value which means it’s most readily utilized by human muscle tissue thus making it a very fast absorbing protein and anabolic as a result. Some users of whey protein concentrate may experience bloating or gas due to its lower quality, but it is very cost effective. Due to its low molecular weight, the higher quality isolate and hydrolysate forms are easier to absorb preventing any digestion pitfalls.
A properly selected whey isolate contains high amounts of ßeta-lactoglobulin, alpha-lactalbumin, Glycomacropeptides, Immunoglobulins, Bovine Serum Albumin, Lactoferrin, Lactoperoxidase, Lysozyme and a high amino acid profile. All of these elements are very important to heavy training athletes, as these compounds can aid in reducing the risk of over training and aid in the digestion process. Whey isolate also gives a quick “boost” in aminos due to its easy and rapid digestion, especially useful in post training when the body needs those aminos to replenish itself. However, it is not a singular source of all the aminos needed to optimally repair broken down muscle tissue.
Quality whey protein isolate provides key microfractions, has a very high concentration of BCAAs for positive effect on lean muscle mass and lower muscle breakdown (whey protein contains about 25% BCAAs—the highest of any protein source), enhances glutathione levels in the body (glutathione is the body’s most powerful natural antioxidant and is a key part of the immune system), features high digestibility and absorption rate, contains virtually no lactose and very low fat, and provides about 50% of the essential amino acids.
Whey protein, a milk derivative, is by far the most popular protein on the market and comes in various forms, from the lower grade, higher fat whey concentrate to the highly purified isolate or hydrolysate form (the latter of which provides the benefits of microfractions and is low in fat and lactose). Most of the whey protein on the market is usually found as ion-exchange, a process using electric charges to extract the protein. There are some advanced procedures (like cross flow microfiltration) that produce higher quality whey, with subsequent added benefits over ion-exchange whey isolate in preserving key microfractions which are essential to its benefits. Whey protein isolate that is not heat-treated contains key microfractions, like alpha lactalbumin and glycomacropeptides, which can both positively support immune function. Some of the microfractions or growth factors found in whey protein can even enhance IGF-1 levels which can increase lean muscle mass—good news for hard training athletes. Whey protein has a very high biological value which means it’s most readily utilized by human muscle tissue thus making it a very fast absorbing protein and anabolic as a result. Some users of whey protein concentrate may experience bloating or gas due to its lower quality, but it is very cost effective. Due to its low molecular weight, the higher quality isolate and hydrolysate forms are easier to absorb preventing any digestion pitfalls.
A properly selected whey isolate contains high amounts of ßeta-lactoglobulin, alpha-lactalbumin, Glycomacropeptides, Immunoglobulins, Bovine Serum Albumin, Lactoferrin, Lactoperoxidase, Lysozyme and a high amino acid profile. All of these elements are very important to heavy training athletes, as these compounds can aid in reducing the risk of over training and aid in the digestion process. Whey isolate also gives a quick “boost” in aminos due to its easy and rapid digestion, especially useful in post training when the body needs those aminos to replenish itself. However, it is not a singular source of all the aminos needed to optimally repair broken down muscle tissue.
Quality whey protein isolate provides key microfractions, has a very high concentration of BCAAs for positive effect on lean muscle mass and lower muscle breakdown (whey protein contains about 25% BCAAs—the highest of any protein source), enhances glutathione levels in the body (glutathione is the body’s most powerful natural antioxidant and is a key part of the immune system), features high digestibility and absorption rate, contains virtually no lactose and very low fat, and provides about 50% of the essential amino acids.
Hydrolyzed Whey Protein
The process of hydrolysis breaks the protein chains down into smaller segments called peptides. Hydrolyzed whey protein is more easily digested and has a reduced potential for allergic reactions versus non-hydrolyzed whey protein. The quality of the protein, however, remains very high. Sports nutrition products and infant formulas often use hydrolyzed whey protein for these reasons. A recent clinical study also found that a specific type of hydrolyzed whey protein was helpful in lowering blood pressure.Whey Protein References
Hoerr R.A., Bostwick E.F., 2000. “Bioactive proteins and probiotic bacteria: modulators of nutritional health.” Nutrition, July-August, 16(7-8): 711-713
Boirie, Y., et al., 1997. “Slow and fast dietary proteins differently modulate post-prandial protein accretion.” Proceedings of the National Academy of Sciences, 94:14930-14935.
Dangin, M., Boirie, Y., Guillet, C., and Beaufrere, B. 2002. “Influence of the protein digestion rate on protein turnover in young and elderly subjects.” Journal of Nutrition, October, 132:3228S-3233S.y of Sciences, 94:14930-14935.
Tolia, V., Lin, C., and Kuhns, L. 1992. “Gastric emptying using three different formulas in infants with gastroesophaegeal reflux.” Journal of Pediatric Gastroenterology and Nutrition, 15(3):297-301.
Appel, L. et. al., 1997. “A clinical trial of the effects of dietary patterns on blood pressure.” The New England Journal of Medicine, 336(16):1117-1124.
FitzGerald, R.J., Meisel, H., 1999. “Lactokinins: Whey protein-derived ACE inhibitory peptides.” Nahrung 43:165-167.
FitzGerald, R.J., Meisel, H., 2000. “Milk protein-derived peptide inhibitors of angiotensin -1-converting enzyme.” British Journal of Nutrition. 84:S33-S37.
Groziak S.M, Miller G.D., 2000. “Natural bioactive substances in milk and colostrum: effects on the arterial blood pressure system.” British Journal of Nutrition, Supplement, November, 84(1):S119-S125.
Esmarck, J.L., Andersen, Olsen, S., Richter, E.A., Mizuno, M., and Kjaer, M., 2001, “Timing of postexercise protein intake is important for muscle hypertrophy with resistance training in elderly humans.” Journal of Physiology, 535.1:301-311.
McCarron, D.A., 1998. “Diet and high blood pressure – the paradigm shift.” Science, 281:933.
McCarron, D. A., 2000. “Dietary calcium and blood pressure control: lessons learned from controlled clinical trials.” Bulletin of the International Dairy Federation, 353:6-9.
Miller, G.D. et al., 2000. “Benefits of dairy product consumption on blood pressure in humans: a summary of the biomedical literature.” Journal of the American College of Nutrition, April 19 (2 Suppl): S147-S164.
Mullally, M., Meisel, H. and Fitzgerald, R., 1997. “Angiotensin-I-Converting enzyme inhibitory activities of gastric and pancreatic proteinase digests of whey proteins.” International Dairy Journal, 7:299-303.
Pfeuffer, M., Schrezenmeir, J., 2000. “Bioactive substances in milk with properties decreasing risk of cardiovascular diseases.” British Journal of Nutrition, Supplement, 84(1):S155-S159.
Pihlanto-Leppala, A. et.al., 2000. “Angiotensin I-converting enzyme inhibitory properties of whey protein digest: concentration and characterization of active peptides.” Journal of Dairy Research, 67:53-64.
Pins, J., and Keenan, J., 2002. “The antihypertensive effects of a hydrolyzed whey protein isolate supplement (BioZate 1®).” Cardiovascular Drugs and Therapy, 16(Supp. 1):68.
Rutherford, K. J., Gill, H.S., 2000. “Peptides affecting coagulation.” British Journal of Nutrition, 84:S99-S102.
Sharpe, S.J., Gamble, G.D., Sharpe, D.N., 1994. “Cholesterol-lowering and blood pressure effect of immune milk.” American Journal of Clinical Nutrition, 59:929-934.
Bounous, G., 2000. “Whey protein concentrate (WPC) and glutathione modulation in cancer treatment.” Anticancer Research, 20:4785-4792.
Bounous, G., Baptist, G., and Gold, P., 1991. “Whey proteins in cancer prevention.” Cancer Letters 57:91. Hakkak, R., Korourian, S., Shelnutt, S. R., et. al., 2000. “Diets containing whey proteins or soy protein isolate protect against 7,12-Dimethylbenz (a) anthracene-induced mammary tumors in female rats.” Cancer Epidemiology, Biomarkers & Prevention, 9:113-117.
Hakkak, R., Korourian, S., Ronis, M.J., Johnston, J., and Badger, T., 2001. “Dietary whey protein protects against azoxymethand-induced colon tumors in male rats.” Cancer Epidemiology, Biomarkers & Prevention, 10:555-558.
Kennedy, R. et. al., 1995. “The use of a whey protein concentrate in the treatment of patients with metastatic carcinoma: A phase I-II clinical study.” Anticancer Research, 15:2643-2650.
McIntosh, G.H., et al., 1995. “Dietary proteins protect against dimethylhydrazine-induced intestinal cancers in rats.” Journal of Nutrition, 125:809-816.
Takada, Y., Aoe, S., Kumegawa, M., 1996. “Whey protein stimulates the proliferation and differentiation of osteoblastic MC3T3-E1 Cells.” Biochemical and Biophysical Research Communications, 223:445-449.
Tsai, W., Chang, W., Chen, C.H., and Lu, F., 2000. “Enhancing effect of patented whey protein isolate (Immunocal) on the cytotoxicity of anti-cancer drug.” Nutrition and Cancer, 38(2):200-208.
Tsuda, H., et al, 2000. “Milk and dairy products in cancer prevention: focus on bovine lactoferrin.” Mutation Research, 462:227-233.
Bounous, G., Gervais, F., Amer, V., Batist, G., Gold, P., 1989. “The influence of dietary protein on tissue glutathione and the diseases of aging.” Clinical Investigative Medicine, 12, 6:343.
Bounous, G, Gold, P., 1991. “The biological activity of undenatured dietary whey proteins: role of glutathione.” Clinical Investigative Medicine, 14(4):296-309.
Bounous, G. et. al., 1989. “Immunoenhancing property of dietary whey protein in mice: role of glutathione.” Clinical Investigative Medicine, 12:154-161.
Bounous, G., Molson, J., 1999. “Competition for glutathione precursors between the immune system and the skeletal muscle: Pathogenesis of chronic fatigue syndrome.” Medical Hypothesis, 53(4):347-349.
Docena, G.H. et. al., 1996. “Identification of casein as the major allergenic and antigenic protein in cow’s milk.” Allergy, 51(6):412-416.
Kennedy, R.S., Bounous, G., Konok, G.P., Baruchel, S., Lee, T.D.G., 1995. “The use of a whey protein concentrate in the treatment of patients with metastatic carcinoma: A phase I-II Clinical Study.” Anticancer Research, 15:2643-2650.
Kuwata, H. et.al., 1998. “Direct evidence of the generation in human stomach of anti-microbial peptide domain(lactoferricin) from ingested lactoferrin.” Biochem. Biophys Acta, 1429:129-141.
LeBoucher, J. et al., 1999. “Modulation of immune response with ornithine A-ketoglutarate in burn injury: an arginine or glutamine dependency?” Nutrition, October, 15(10):773-777.
Wang, H., Ye, X., Ng, T.B., 2000. “First demonstration of an inhibitory activity of milk proteins against human immunodeficiency virus-1 reverse transcriptase and the effect of succinylation.” Life Sciences, 67:2745-2752.
Wong, C.W. et al., 1997. “Effects of purified bovine whey factors on cellular immune functions in ruminants.” Veterinary Immunology and Immunopathology, 56:85-96.
Lemon, W.R. et al, 1996. “Is increased dietary protein necessary or beneficial for individuals with a physically active lifestyle?” Nutrition Reviews Supplement, 54:S169-175.
Lemon, W.R., 1998. “Effects of exercise on dietary protein requirements.” International Journal of Sport Nutrition and Exercise Metabolism, 8(4): 426-447.
Beeh, M., Schlaak, J.F., Buhl, R., 2001. “Oral supplementation with whey proteins increases plasma glutathione levels of HIV infected patients.” European Journal of Clinical Investigation, February, 31 (2):171-178.
Berkhout, B. et al., 2002. “Characterization of the anti-HIV effects of native lactoferrin and other milk proteins and protein-derived peptides.” Antiviral Research, 55:341-355.
Bounous, G. et. al., 1991. “Whey protein as a food supplement in HIV-seropositive individuals.” Clinical Investigative Medicine, 16(3):204-209.
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