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Fact: As protein intake increases the influence of protein quality decreases. In other words, high quantity can significantly make up for low quality. The quantity of protein in the diet may in fact add importance to the scoring assessment of a given protein. In fact, if you only eat 35- 45 grams a protein a day you better make sure you chose the highest quality protein you can find. On the other hand, if you eat quantities of protein common among bodybuilders, say 1.6 - 1.8 grams per kilogram, the large amount of amino acids overcome slight differences in scoring. Once you achieve a certain levels of quality in a protein supplement, increasing it further will not significantly change it¹s effectiveness when consumed in quantities sufficient to pack on muscle. Here is a quick overview of the various methods used to determine protein quality. Keep in mind that tests used to determine protein quality use the lower threshold of protein requirements. This creates a metabolic environment far different from that seen in a well fed bodybuilder or athlete. Chemical Scoring Although it is relatively easy and inexpensive to do a chemical scoring of any protein, it does not always accu-rately predict how well the body can utilize it. So the ad-vantages of chemical scoring in determining the quality of protein are that it is easy and inexpensive. It's drawback is that it cannot tell you anything about the digestibility of the protein. Chemical scoring also involves a procedure that may destroy certain amino acids and this may lead to inaccurate values. It is also insensitive to substances in a given protein that can adversely effect digestibility. To discover this variable the test would have to utilize living animals. Biological value (BV) When measuring the BV of a protein source, two nitrogen studies are done. The first study determines how much nitrogen is lost from the body even when no protein is fed. This amount of nitrogen loss is assumed to be inevitable and that the body will naturally lose it regardless of the amount of nitrogen in the diet. In the second study an amount of the protein is fed that is slightly below what is required. As before, the nitrogen losses are then measured, but this time they are compared to the amount of nitrogen consumed. To determine the actual BV of the protein the re-sults are then derived using this formula:
This method often involves animal test subjects and is more frequently used. It's draw backs are that if a low NPU is obtained, it is impossible to know if it is because of a poor amino acid profile or low digestibility. Protein efficiency Ratio (PER)
The benefits of this method are it's expense and simplicity. It's drawbacks are that it is time consuming; the amino acid needs of rats are not those of humans; and the amino acid needs of growing animals are not those of adult animals (growing animals and humans need more lysine, for example). The PER is used to qualify statements about daily pro-tein requirement in the United States. You are assumed to eat protein with a PER that is equal to or better than that of the milk protein casein; if the protein's PER is lower, you must eat more of it to meet the RDA. Food labels have to take protein quality into consideration, using the PER of casein as a reference point. If a food has a protein quality equal or better than that of casein, the RDA is 45 grams. If the protein quality is less than casein you need 65 grams for the RDA. You may be wondering if it makes any difference if you eat your protein from a supplement or from food. Remember that by the time it gets absorbed into the blood stream, all your body knows is how much of each amino acid was present in the food you ate. If you have the money, it is certainly convenient to just drink down a high quality protein supplement. Beyond that, it makes no difference in what form you get your protein from as long as its a complete protein and sufficiently digestible. Protein digestibility-corrected amino acid score
(PDCAA) Some foods however, contain anti-nutritional factors. These factors sometimes occur naturally like in some beans, or are a result of heating and/or cooking, and inhibit the ability of the body to digest and thus absorb certain amino acids. Research has shown the PDCAA method of scoring protein often over estimates the quality of foods containing anti-nutritional factors.12 The take home message from all this is that arguments about who¹s protein scored highest on this test or that test are really meaningless to the average well fed athlete.
Conclusion
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| References: 1. Tipton K., Ferrando A., Phillips S., Doyle, JR D., Wolfe R. Post exercise net protein synthesis in human muscle from orally administered amino acids. Am. J. Physiol. 276: E628-E634, 1999 2. Bennet, W. M., A. A. Connacher, C. M. Scrimgeour, and M. J. Rennie. The effect of amino-acid infusion on leg protein turnover assessed by L-[15N]phenylalanine and L-[1-13C]leucine exchange. Eur. J. Clin. Invest. 20: 37-46, 1989 3. Castellino, P., L. Luzi, D. C. Simonson, M. Haymond, and R. A. DeFronzo. Effect of insulin and plasma amino acid concentrations on leucine metabolism in man. J. Clin. Invest. 80: 1784-1793, 1987 4. Fryburg, D. A., L. A. Jahn, S. A. Hill, D. M. Oliveras, and E. J. Barrett. Insulin and insulin-like growth factor-I enhance human skeletal muscle protein anabolism during hyperaminoacidemia by different mechanisms. J. Clin. Invest. 96: 1722-1729, 1995 5. McNulty, P. H., L. H. Young, and E. J. Barrett. Response of rat heart and skeletal muscle protein in vivo to insulin and amino acid infusion. Am. J. Physiol. 264 (Endocrinol. Metab. 27): E958-E965, 1993 6. Mosoni, L., M. Houlier, P. P. Mirand, G. Bayle, and J. Grizard. Effect of amino acids alone or with insulin on muscle and liver protein synthesis in adult and old rats. Am. J. Physiol. 264 (Endocrinol. Metab. 27): E614-E620, 1993 7. Newman, E., M. J. Heslin, R. F. Wolf, P. T. W. Pisters, and M. F. Brennan. The effect of systemic hyperinsulinemia with concomitant infusion of amino acids on skeletal muscle protein turnover in the human forearm. Metabolism 43: 70-78, 1994 8. Watt, P. W., M. E. Corbett, and M. J. Rennie. Stimulation of protein synthesis in pig skeletal muscle by infusion of amino acids during constant insulin availability. Am. J. Physiol. 263 (Endocrinol. Metab. 26): E453-E460, 1992 9. Newsholme, A.E., Parry-Billings M. Properties of glutamine release from muscle and its importance for the immune system. JPEN. 14 (4) supplement S63-67 10. Oddoye EA., Margen S. Nitrogen balance studies in humans: long-term effect of high nitrogen intake on nitrogen accretion. J Nutr 109 (3): 363-77 11. Boirie Y, Dangin M, Gachon P, Vasson M-P, Maubois J-L, and Beaufrère B. Slow and fast dietary proteins differently modulate postprandial protein accretion (amino acid turnover / postprandial protein anabolism / milk protein / stable isotopes) Proc. Natl. Acad. Sci. USA Vol. 94, pp. 14930-14935, December 1997 12. Sarwar G. The Protein Digestibility-Corrected Amino Acid Score method overestimates quality of proteins containing antinutritional factors and of poorly digestible proteins supplemented with limiting amino acids in rats. J. Nutr. 127: 758-764, 1997 13. Millward, D.J. Metabolic demands for amino acids and the human dietary requirement: Millward and Rivers (1988) revisited. J. Nutr. 128: 2563S-2576S, 1998 14. Fern EB, Bielinski RN, Schutz Y. Effects of exaggerated amino acid and protein supply in man. Experientia 1991 Feb 15;47(2):168-72 15. Dragan, GI., Vasiliu A., Georgescu E. Effect of increased supply of protein on elite weight-lifters. In:Milk Protein T.E. Galesloot and B.J. Tinbergen (Eds.). Wageningen The Netherlands: Pudoc, 1985, pp. 99-103
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