WHEN YOU EAT PROTEIN WHAT DOES IT DO?
A GUIDE FOR ATHLETES
Part 2 of 4 QUALITY & TYPE OF PROTEIN
Dr Michael Colgan 24 February 2015
Quality of Protein
In my 1981 book, YOUR PERSONAL VITAMIN PROFILE, I documented why meat proteins are effective only if they come from animals fed their natural diet (1). The book became a best seller and, understandably, members of the meat and poultry industries criticized me as, “a nut living in the past”, and “How does Colgan think that farmers could ever afford to go back to those days?” By then, because of stupid US agricultural policies and subsidies of the 1950s, to expand corn, soybean, sugar beet, and wheat farming, about 80% of all cattle, and almost all poultry, had been forced off the land into feedlots and battery farms. I predicted then it would get a lot worse.
In my 2007 book, NUTRITION FOR CHAMPIONS, I document how it has got a lot worse. Since 1950, feedlot and battery farming has progressively degraded livestock, generation after generation (2). Today, this terrible mistake in farming development in North America breeds animal grotesques for our meat. The protein from these degraded animals bear little relation to that of healthy livestock of the early 20th century (2).
Beef is a good example. Designed by evolution to thrive only as grazers roaming open range, most cattle today are confined to stand shoulder to shoulder in their own feces for all their short and brutal lives. Instead of continuous grazing on grassland, the way in which the gut of cattle evolved to work, they are fed intermittently, with unnatural foods, such as chicken feathers.
Cattle evolved for more than 100 million years, to develop a rumen as their main stomach. A rumen is essentially a fermentation tank for grass. To work properly the rumen has to be kept fermenting by constant grazing and movement. Livestock in feedlots are confined in movement, and intermittently fed unnatural foods that their rumens struggle to digest. They cannot operate as evolution designed them. Hence, the progressive degradation of our beef (and milk) proteins for the last 65 years (3).
Corn too, a completely unnatural food for cattle, was so bad from the get-go, that cunning agribusiness had to resort to the old advertising trick of fooling folk into believing that a sin is a virtue. “All corn fed” was distorted into a virtue to seek, rather than the horror it is to avoid. Whenever we test protein from these animal grotesques, its biological value is less than that of GMO soy (2,3).
Hence also, the whole sick spectacle of growth stimulating drugs and antibiotics. These chemicals, including more than five times all the antibiotics used by humans each year, have to be fed, and injected, and stuffed up the fundaments of our beef, just to keep them healthy enough for a 40-week short and ugly life before sending them to slaughter.
As I have documented in previous articles, this veterinary use of antibiotics is largely responsible for the massive increase in antibiotic resistant infections, such as MRSA, that now plague our hospitals. If you want to achieve your athletic potential, do not allow any of this meat into your nutrition.
Now, thanks to numerous books and articles and constant complaints to government by thousands of scientists, including me, rumens are starting to churn happily again, and “organic grass-fed” and “organic free-range” meats have reappeared in our supermarkets (3,4). They are not as good as wild meats, and still do not provide the protein quality of livestock before 1950. Nevertheless, the meat and milk proteins from organic, range-fed livestock, and meat and eggs from organic, free-range poultry, and wild fish, are the best animal sources of protein athletes can get.
Best Form of Protein
Current government criteria compare proteins by what is called the protein-digestibility-corrected- amino-acid-score (PDCAAS). The reference protein is whole egg, the best protein science knew in the 1980s. Whole egg was arbitrarily given a PDCAAS of 1.0, representing 100% digestibility and absorption. Big mistake.
When research on whey proteins began recording scores of 120-140 % compared with whole egg protein, these scores were disallowed by government, because over 100% did not make sense to regulators (5). Consequently, commonly recommended proteins for athletes from whey, casein, egg-white, and fish, were all arbitrarily labelled the same, “high quality”, and capped by regulation with a PCDAAS of 1.0. Bigger mistake.
As research advances, science is self-correcting. Regulations, however, are never self-correcting, and are seldom corrected, even when obviously wrong. On the contrary, regulations are jealously guarded, usually by old men, appointed long after their due-by date, to guard the past. Happily, real science is concerned with the future.
We know now that muscle protein synthesis is largely regulated by the amino acid profile of the protein, especially its content of the three branched-chain amino acids (BCAA), leucine, isoleucine, and valine. Greatest action occurs to leucine, for muscle protein synthesis, and for adaptation to training (6-9), Whey proteins have the highest content of leucine (10).
And it is also leucine alone that has the ability to “switch on” the DNA codes and the cell signaling machinery governing protein synthesis (11,12). Official “high quality” proteins, rated as exactly the same by government, differ greatly in their amino acid profiles. All leading sports scientists I know are well aware that government classification of proteins uses the obsolete science of the 1980s, not the science of today.
In addition to amino acid composition, proteins also differ greatly in their rates of digestion and absorption. How rapidly a protein increases muscle amino acids, especially levels of leucine, regulates the extent of muscle remodeling that night.
Meat and fish proteins, and all solid forms of protein, including most protein bars, are slowly absorbed, Protein dissolved in a drink is better. Nevertheless, common drinks of egg, casein, soy, and mixed vegetable proteins, are all more slowly absorbed than whey protein drinks (13,14).
As an athlete, you need the fastest possible protein to take advantage of what I christened, “the anabolic window”, in 1993 (4). This is the period of about 90 minutes immediately after exercise, during which muscle amino acids are in greatest flux. Muscle can uptake more protein during the anabolic window than at any other time.
To trigger the greatest muscle protein synthesis, all athletes on our program take a 36-gram whey protein shake immediately after each training period. They take the shakes early in the anabolic window, to allow at least 45 minutes for amino acid absorption into muscle.
Most other proteins are too slow, taking two hours or more for absorption. Athletes do best who take 25-40 grams of undenatured, cold extracted, whey protein concentrate, together with its co-factor vitamins and minerals immediately after training. It’s the most rapidly digested and absorbed protein drink that we know (2,4,15,16). Our winning team of athletes from various disciplines, make it the basis of their protein nutrition.
In Part 3 of this series I will cover timing, frequency and amount of protein for optimum sports nutrition.
For the best of sports nutrition and training, join our winning team at drmichaelcolgan.com
1. Colgan M. Your Personal Vitamin Profile. New York: William Morrow, 1981.
2. Colgan M. The Anti-Inflammatory Athlete. Indian Fork UT: Sound Concepts 2012.
3. Colgan M. Nutrition for Champions. Vancouver: Science Books, 2007.
4. Colgan M. Optimum Sports Nutrition. New York: Advanced Research Press, 1993.
5. Schaafsma, G. The protein digestibility-corrected amino acid score. J. Nutr. 2000;130(7): 1865S–1867S. PMID:10867064.
6. Tipton, K.D., and Witard, O.C.. Protein requirements and recommendations for athletes: relevance of ivory tower arguments for practical recommendations. Clin. Sports Med. 2007;26(1): 17–36. doi:10.1016/j.csm.2006.11.003. PMID:17241913.
7. Tipton, K.D., Ferrando, A.A., Phillips, S.M., Doyle, D., Jr., and Wolfe, R.R.. Postexercise net protein synthesis in human muscle from orally administered amino acids. Am. J. Physiol. 1999a 276(4): E628–E634. PMID:10198297.
8. Tipton, K.D., Gurkin, B.E., Matin, S., and Wolfe, R.R.. Nonessential jamino acids are not necessary to stimulate net muscle protein synthesis in healthy volunteers. J. Nutr. Biochem. 1999b; 10(2): 89–95. doi:10.1016/S0955-2863(98)00087-4. PMID:15539275.
9. Phillips, S.M., Tang, J.E., and Moore, D.R. The role of milk- and soy-based protein in support of muscle protein synthesis and muscle protein accretion in young and elderly persons. J. Am. Coll. Nutr. 2009;28(4): 343–354. doi:10.1080/ 07315724.2009.10718096. PMID:20368372.
10. Tang, J.E., Moore, D.R., Kujbida, G.W., Tarnopolsky, M.A., and Phillips, S.M. Ingestion of whey hydrolysate, casein, or soy protein isolate: effects on mixed muscle protein synthesis at rest and following resistance exercise in young men. J. Appl. Physiol. 2009;107(3): 987–992. doi:10.1152/japplphysiol.00076.2009. PMID:19589961.
11. Drummond, M.J., and Rasmussen, B.B.. Leucine-enriched nutrients and the regulation of mammalian target of rapamycin signalling and human skeletal muscle protein synthesis. Curr. Opin. Nutr. Metab. Care. 2008;11(3): 222–226. doi: 10.1097/MCO.0b013e3282fa17fb. PMID: 18403916.
12. Phillips, S.M., and van Loon, L.J. Dietary protein for athletes: From requirements to optimum adaptation. J. Sports Sci. 2011;29(Suppl. 1): S29–S38. doi:10. 1080/02640414.2011.619204. PMID:22150425.
13. Pennings, B., Boirie, Y., Senden, J.M., Gijsen, A.P., Kuipers, H., and van Loon, L.J. Whey protein stimulates postprandial muscle protein accretion more effectively than do casein and casein hydrolysate in older men. Am. J. Clin. Nutr. 2011;93(5): 997–1005. doi:10.3945/ajcn.110.008102. PMID:21367943.
14. Pennings, B., Groen, B., de Lange, A., Gijsen, A.P., Zorenc, A.H., Senden, J.M., and van Loon, L.J. Amino acid absorption and subsequent muscle protein accretion following graded intakes of whey protein in elderly men. Am. J. Physiol. Endocrinol. Metab. 2012;302(8): E992–E999. doi:10.1152/ajpendo.00517. 2011. PMID:22338070.
15. Breen, L., Philp, A., Witard, O.C., Jackman, S.R., Selby, A., Smith, K., et al. The influence of carbohydrate-protein co-ingestion following endurance exercise on myofibrillar and mitochondrial protein synthesis. J. Physiol. 2011;589(16): 4011–4025. doi:10.1113/jphysiol.2011.211888. PMID:21746787.
16. West, D.W., Burd, N.A., Coffey, V.G., Baker, S.K., Burke, L.M., Hawley, J.A., et al. Rapid aminoacidemia enhances myofibrillar protein synthesis and anabolic intramuscular signaling responses after resistance exercise. Am. J. Clin. Nutr. 2011;94(3): 795–803. doi:10.3945/ajcn.111.013722. PMID:21795443.
A GUIDE FOR ATHLETES
Part 2 of 4 QUALITY & TYPE OF PROTEIN
Dr Michael Colgan 24 February 2015
Quality of Protein
In my 1981 book, YOUR PERSONAL VITAMIN PROFILE, I documented why meat proteins are effective only if they come from animals fed their natural diet (1). The book became a best seller and, understandably, members of the meat and poultry industries criticized me as, “a nut living in the past”, and “How does Colgan think that farmers could ever afford to go back to those days?” By then, because of stupid US agricultural policies and subsidies of the 1950s, to expand corn, soybean, sugar beet, and wheat farming, about 80% of all cattle, and almost all poultry, had been forced off the land into feedlots and battery farms. I predicted then it would get a lot worse.
In my 2007 book, NUTRITION FOR CHAMPIONS, I document how it has got a lot worse. Since 1950, feedlot and battery farming has progressively degraded livestock, generation after generation (2). Today, this terrible mistake in farming development in North America breeds animal grotesques for our meat. The protein from these degraded animals bear little relation to that of healthy livestock of the early 20th century (2).
Beef is a good example. Designed by evolution to thrive only as grazers roaming open range, most cattle today are confined to stand shoulder to shoulder in their own feces for all their short and brutal lives. Instead of continuous grazing on grassland, the way in which the gut of cattle evolved to work, they are fed intermittently, with unnatural foods, such as chicken feathers.
Cattle evolved for more than 100 million years, to develop a rumen as their main stomach. A rumen is essentially a fermentation tank for grass. To work properly the rumen has to be kept fermenting by constant grazing and movement. Livestock in feedlots are confined in movement, and intermittently fed unnatural foods that their rumens struggle to digest. They cannot operate as evolution designed them. Hence, the progressive degradation of our beef (and milk) proteins for the last 65 years (3).
Corn too, a completely unnatural food for cattle, was so bad from the get-go, that cunning agribusiness had to resort to the old advertising trick of fooling folk into believing that a sin is a virtue. “All corn fed” was distorted into a virtue to seek, rather than the horror it is to avoid. Whenever we test protein from these animal grotesques, its biological value is less than that of GMO soy (2,3).
Hence also, the whole sick spectacle of growth stimulating drugs and antibiotics. These chemicals, including more than five times all the antibiotics used by humans each year, have to be fed, and injected, and stuffed up the fundaments of our beef, just to keep them healthy enough for a 40-week short and ugly life before sending them to slaughter.
As I have documented in previous articles, this veterinary use of antibiotics is largely responsible for the massive increase in antibiotic resistant infections, such as MRSA, that now plague our hospitals. If you want to achieve your athletic potential, do not allow any of this meat into your nutrition.
Now, thanks to numerous books and articles and constant complaints to government by thousands of scientists, including me, rumens are starting to churn happily again, and “organic grass-fed” and “organic free-range” meats have reappeared in our supermarkets (3,4). They are not as good as wild meats, and still do not provide the protein quality of livestock before 1950. Nevertheless, the meat and milk proteins from organic, range-fed livestock, and meat and eggs from organic, free-range poultry, and wild fish, are the best animal sources of protein athletes can get.
Best Form of Protein
Current government criteria compare proteins by what is called the protein-digestibility-corrected- amino-acid-score (PDCAAS). The reference protein is whole egg, the best protein science knew in the 1980s. Whole egg was arbitrarily given a PDCAAS of 1.0, representing 100% digestibility and absorption. Big mistake.
When research on whey proteins began recording scores of 120-140 % compared with whole egg protein, these scores were disallowed by government, because over 100% did not make sense to regulators (5). Consequently, commonly recommended proteins for athletes from whey, casein, egg-white, and fish, were all arbitrarily labelled the same, “high quality”, and capped by regulation with a PCDAAS of 1.0. Bigger mistake.
As research advances, science is self-correcting. Regulations, however, are never self-correcting, and are seldom corrected, even when obviously wrong. On the contrary, regulations are jealously guarded, usually by old men, appointed long after their due-by date, to guard the past. Happily, real science is concerned with the future.
We know now that muscle protein synthesis is largely regulated by the amino acid profile of the protein, especially its content of the three branched-chain amino acids (BCAA), leucine, isoleucine, and valine. Greatest action occurs to leucine, for muscle protein synthesis, and for adaptation to training (6-9), Whey proteins have the highest content of leucine (10).
And it is also leucine alone that has the ability to “switch on” the DNA codes and the cell signaling machinery governing protein synthesis (11,12). Official “high quality” proteins, rated as exactly the same by government, differ greatly in their amino acid profiles. All leading sports scientists I know are well aware that government classification of proteins uses the obsolete science of the 1980s, not the science of today.
In addition to amino acid composition, proteins also differ greatly in their rates of digestion and absorption. How rapidly a protein increases muscle amino acids, especially levels of leucine, regulates the extent of muscle remodeling that night.
Meat and fish proteins, and all solid forms of protein, including most protein bars, are slowly absorbed, Protein dissolved in a drink is better. Nevertheless, common drinks of egg, casein, soy, and mixed vegetable proteins, are all more slowly absorbed than whey protein drinks (13,14).
As an athlete, you need the fastest possible protein to take advantage of what I christened, “the anabolic window”, in 1993 (4). This is the period of about 90 minutes immediately after exercise, during which muscle amino acids are in greatest flux. Muscle can uptake more protein during the anabolic window than at any other time.
To trigger the greatest muscle protein synthesis, all athletes on our program take a 36-gram whey protein shake immediately after each training period. They take the shakes early in the anabolic window, to allow at least 45 minutes for amino acid absorption into muscle.
Most other proteins are too slow, taking two hours or more for absorption. Athletes do best who take 25-40 grams of undenatured, cold extracted, whey protein concentrate, together with its co-factor vitamins and minerals immediately after training. It’s the most rapidly digested and absorbed protein drink that we know (2,4,15,16). Our winning team of athletes from various disciplines, make it the basis of their protein nutrition.
In Part 3 of this series I will cover timing, frequency and amount of protein for optimum sports nutrition.
For the best of sports nutrition and training, join our winning team at drmichaelcolgan.com
1. Colgan M. Your Personal Vitamin Profile. New York: William Morrow, 1981.
2. Colgan M. The Anti-Inflammatory Athlete. Indian Fork UT: Sound Concepts 2012.
3. Colgan M. Nutrition for Champions. Vancouver: Science Books, 2007.
4. Colgan M. Optimum Sports Nutrition. New York: Advanced Research Press, 1993.
5. Schaafsma, G. The protein digestibility-corrected amino acid score. J. Nutr. 2000;130(7): 1865S–1867S. PMID:10867064.
6. Tipton, K.D., and Witard, O.C.. Protein requirements and recommendations for athletes: relevance of ivory tower arguments for practical recommendations. Clin. Sports Med. 2007;26(1): 17–36. doi:10.1016/j.csm.2006.11.003. PMID:17241913.
7. Tipton, K.D., Ferrando, A.A., Phillips, S.M., Doyle, D., Jr., and Wolfe, R.R.. Postexercise net protein synthesis in human muscle from orally administered amino acids. Am. J. Physiol. 1999a 276(4): E628–E634. PMID:10198297.
8. Tipton, K.D., Gurkin, B.E., Matin, S., and Wolfe, R.R.. Nonessential jamino acids are not necessary to stimulate net muscle protein synthesis in healthy volunteers. J. Nutr. Biochem. 1999b; 10(2): 89–95. doi:10.1016/S0955-2863(98)00087-4. PMID:15539275.
9. Phillips, S.M., Tang, J.E., and Moore, D.R. The role of milk- and soy-based protein in support of muscle protein synthesis and muscle protein accretion in young and elderly persons. J. Am. Coll. Nutr. 2009;28(4): 343–354. doi:10.1080/ 07315724.2009.10718096. PMID:20368372.
10. Tang, J.E., Moore, D.R., Kujbida, G.W., Tarnopolsky, M.A., and Phillips, S.M. Ingestion of whey hydrolysate, casein, or soy protein isolate: effects on mixed muscle protein synthesis at rest and following resistance exercise in young men. J. Appl. Physiol. 2009;107(3): 987–992. doi:10.1152/japplphysiol.00076.2009. PMID:19589961.
11. Drummond, M.J., and Rasmussen, B.B.. Leucine-enriched nutrients and the regulation of mammalian target of rapamycin signalling and human skeletal muscle protein synthesis. Curr. Opin. Nutr. Metab. Care. 2008;11(3): 222–226. doi: 10.1097/MCO.0b013e3282fa17fb. PMID: 18403916.
12. Phillips, S.M., and van Loon, L.J. Dietary protein for athletes: From requirements to optimum adaptation. J. Sports Sci. 2011;29(Suppl. 1): S29–S38. doi:10. 1080/02640414.2011.619204. PMID:22150425.
13. Pennings, B., Boirie, Y., Senden, J.M., Gijsen, A.P., Kuipers, H., and van Loon, L.J. Whey protein stimulates postprandial muscle protein accretion more effectively than do casein and casein hydrolysate in older men. Am. J. Clin. Nutr. 2011;93(5): 997–1005. doi:10.3945/ajcn.110.008102. PMID:21367943.
14. Pennings, B., Groen, B., de Lange, A., Gijsen, A.P., Zorenc, A.H., Senden, J.M., and van Loon, L.J. Amino acid absorption and subsequent muscle protein accretion following graded intakes of whey protein in elderly men. Am. J. Physiol. Endocrinol. Metab. 2012;302(8): E992–E999. doi:10.1152/ajpendo.00517. 2011. PMID:22338070.
15. Breen, L., Philp, A., Witard, O.C., Jackman, S.R., Selby, A., Smith, K., et al. The influence of carbohydrate-protein co-ingestion following endurance exercise on myofibrillar and mitochondrial protein synthesis. J. Physiol. 2011;589(16): 4011–4025. doi:10.1113/jphysiol.2011.211888. PMID:21746787.
16. West, D.W., Burd, N.A., Coffey, V.G., Baker, S.K., Burke, L.M., Hawley, J.A., et al. Rapid aminoacidemia enhances myofibrillar protein synthesis and anabolic intramuscular signaling responses after resistance exercise. Am. J. Clin. Nutr. 2011;94(3): 795–803. doi:10.3945/ajcn.111.013722. PMID:21795443.
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