Sunday, 29 March 2015

Dr Michael Colgan - Daily Amounts of protein - Part 3



Dr Michael Colgan 4 March 2015
In response to the unexpected hundreds of questions from readers, I have to review where we are in this series. In Part 1, I documented the huge advances in the Proteome Project since 2005, confirming how protein is far and away the most complex nutrient in your diet (1).

You Are a Protein Machine
We know now that food proteins provide the environmental signals to release the DNA codes for over 350,000 different proteins that compose every working unit in your body. All other nutrients, essential fats, carbohydrates, vitamins, and minerals are simply supports for your protein system (1). There is no controversy regarding this science. It is accepted by all major scientists I know.
Food proteins provide not only the signals to your DNA, but also provide the raw materials to make each of your body proteins, in response to the release of its code. Each body protein code is precise. Different proteins can differ from each other by many thousands of lines of code. Your structure is built of, and you are operated by, these proteins. The quality of the protein you eat, determines the quality of the proteins that compose all the muscles that move you, and all the brain cells that operate your mind (2).

You Are Controlled by Light
I also explained how the manufacture, life, and regular death of all the proteins that compose us, (and all other creatures), developed under the tight control of light. This first occurred when life began on Earth over 400 million years ago. The life of all our proteins is still controlled by light today (3,4). By stimulating an area called the suprachiasmatic nucleus in our brains, the changing light of the revolution of the Earth, imposes a circadian rhythm which controls every aspect of human biology, 24 hours a day, including the birth, and life, and death of all our proteins. To achieve optimum performance, the quality, type, amount, timing, and frequency of your protein nutrition, and its integration with athletic training, have to be in synchrony with this circadian rhythm (3,4). In combination with correct training, protein nutrition provides what we first termed THE ADAPTIVE STIMULUS in 1982. The body responds to the adaptive stimulus each night to repair and remodel the muscles stimulated by exercise that day. To achieve best results, the adaptive stimulus must be provided EVERY DAY. Otherwise, that particular circadian cycle finishes that night with little remodeling of muscle, and that day’s opportunity for growth of muscle and strength is lost forever (3,4).

Most Proteins Now DegradedIn Part 2, I explained how the bulk of proteins in America, from livestock, poultry, (and farmed fish) has been progressively degraded since 1950. Stupid errors in government farming policies - now constantly denied and swept under the Washington carpet - have forced most animals off the land into feedlots and battery farms. Over the last 65 years, they have been fed unnatural diets, and inbred into animal grotesques (5). These degraded animals provide proteins so inferior they have no place in the athlete’s diet. Eat battery chicken for your protein and you will devolve progressively into a battered chicken. You will run with battered chicken legs, and think with a battered chicken brain. Even if you manage to retain sufficient wits to change to a healthy protein diet, it will take several years to undo the damage (5).High BCAA Whey Proteins BestI also showed why the government classification of complete proteins by the PDCAAS system, developed in the 1970s, is obsolete and untenable (6). The PDCASS is retained today only to support agribusiness profits. I documented how modern science shows clearly that incorporation of a food protein into muscles, organs, and brain, depends on its amino acid profile (7-10 ). Proteins with the highest content of the three branched-chain amino acids (BCAA), leucine, isoleucine, and valine, are incorporated into muscle best. Leucine however, is the sole amino acid able to trigger the DNA code system to release the codes for many muscle proteins. Whey proteins have the highest content of leucine, making whey the amino acid profile of choice (7-11 ).

Proteins also differ greatly in their speed of digestion and absorption into muscle. The fastest proteins yield the greatest muscle recovery and growth (7-12). Solid proteins from meat, fish, eggs, cheese, and vegetables are slowly digested and absorbed over 2-4 hours. Almost all protein bars, especially bars high in casein or soy, and all casein and soy drinks, are also slowly digested and absorbed over 2-3 hours. Whey protein concentrate dissolved into a drink is rapidly digested and absorbed, over about 45 minutes, making whey an ideal protein source for athletes (7-13). Whey is also the only commonly available protein that can take advantage of the 90-minute ANABOLIC WINDOW immediately after training. This is the crucial period we first identified in 1992, during which muscle will take up more protein than at any other time (2).

Cold MAP Processing EssentialThe whey, however, has to be from range-fed animals eating their natural diet, and also has to remain undenatured. That is, it must be cold-extracted and minimally processed, using what is termed, modified-atmospheric-protection (MAP) technology. MAP technology excludes light, heat, moisture and air (2).

Range-fed cows, cold-extraction, and MAP processing, are essential to maintain the quality of the whey: to preserve its amino acid profile, sulfur bonds, di-peptides, tri-peptides, and live immunoglobulins. Most commercial whey proteins do not fulfill these conditions.

Unfortunately bogus claims are rampant on ads and labels, owing to the lack of government control of protein, which can be sold freely as a food. Food labelling was initially meant to be an exercise in revelation, to inform the public what they are buying. Over the years, it has become largely an exercise in deception.

If you buy nutritional supplements by comparing labels, you have fallen for this deception. Buy only from companies with a long-term, spotless reputation, companies with a reputation to lose. Remember, you can buy a watch that looks like a Rolex in any airport for $20. But a real Rolex costs at least $4,000. It is the same with protein. The real thing is likely to be expensive, but worth every penny.

Integrity of Protein Must Remain Until You Eat ItThe exclusion of light, heat, moisture, and air has to prevail until you eat the protein. Once opened, all tubs of protein powder immediately begin to oxidize. Just like an opened bottle of wine, once opened, tubs of protein quickly spoil, and lose their ability to build muscle or brain. This basic science is well appreciated by biochemists who have to prevent oxidation, in the laboratory. But about 90% of protein powders now on the market do nothing to prevent oxidation, and are next to useless for athletes.
Oxidized protein is a major reason why results from using many protein powders are generally poor to none. It is also why all athletes on Colgan Institute programs only use shakes made with whey protein powders sold in single-serve, sealed, opaque, foil or plastic packets. If kept cool and dry, these remain good for two years on the shelf.

Daily Amount of ProteinThe next question is how much protein to use every day. Modern science has long since rejected the obsolete, government stipulation of 0.8 grams per kilogram bodyweight per day. Controlled studies show clearly that this level of protein intake leaves even moderate exercisers in chronic deficit (14).

Back in the 1980s, we calculated from basic principles of biology that maximum muscle remodeling in lean athletes would occur at an average intake of top quality protein of 1.8 grams per kilogram bodyweight per day (15). Actual measures of nitrogen retention in lean, fit, young men doing intense exercise, by protein expert Dr Peter Lemon at Kent State U, showed maximum incorporation of protein into muscle of at 1.7 grams per kilogram bodyweight, almost identical to our theoretical calculations (16).

For a lean athlete of 70 kg (154 lbs), in hard training, that is about 130 grams of top quality protein each day. In the Colgan Power Program, it equates to three of our 36-gram shakes of whey protein concentrate, plus two small meals of free-range meats or eggs, wild meats, or wild fish, plus unlimited organic vegetables, seeds, and nuts, each day.

We generally eat little to no grains, milk, cheese, or sugars. Two of the protein shakes are taken immediately after training, as all our athletes train twice per day, six days a week. (Seventh day is light training only.)

More recently, respected sports scientists have done meta-analyses of the best controlled studies. Results indicate that additional remodeling of muscle, plus remodeling of gut, vascular, and mitochondrial proteins, continues to occur over 24 hours after training, with timed protein intakes up to 2.4 grams per kilogram lean mass per day (17-19). There are no reported side-effects from this level of intake, rather, considerable benefits.

This high level of protein is especially suitable for power athletes, such as weightlifters, bodybuilders, powerlifters, football players, and field athletes, whose training is focused on maximum muscle and strength. For an athlete of 70kg (154 lbs), that is about 170 grams of top quality protein per day. In the Colgan Power Program, it equates to four of our 36-gram shakes of whey protein concentrate, plus two small meals of free-range meats, or wild meats, or wild fish, per day. Excepting for potatoes, that are all now degraded in the US, we eat vegetables, nuts and seeds freely.

Eat between 1.8 and 2.4 grams of top quality protein per kilogram lean weight per day. In conjunction with the right timing and frequency of intake, and the right training, it will provide the adaptive stimulus you need to release the enormous genetic power you have latent in your genes.
I will cover the optimum timing and frequency of protein nutrition, and its integration with training, in Part 4.

Thanks a million for the huge response to this series, over 80,000 hits on our pages and blogs in the last week, and for the enormous number of great questions. The only way I can answer readers is to add a little more depth to each short article in the series. I will enjoy revealing the new findings of sports science, that I am confident will help you release your athletic potential. Go for the gold ! It is waiting in your genes.

If you believe you can be a fit for our winning team, go to,

1. Wang K, Huang C, Nice E. Recent advances in proteomics: towards the human proteome. Biomed Chromatogr. 2014 Jun;28(6):848-57. doi: 10.1002/bmc.3157. Review.2. Colgan M. Optimum Sports Nutrition. New York: Advanced Research Press, 1993.3. Erren TC, et al. Light, timing of biological rhythms and chronodisruption in man. Naturwissenschaften, 2003;90:485-494.4. Dawson KA. Temporal organization of the brain: Neurocognitive mechanisms and clinical applications. Brain Cogn, 2004;54:75-94.5. Colgan M. Nutrition for Champions. Vancouver: Science Books, 2007.6. Schaafsma, G. The protein digestibility-corrected amino acid score. J. Nutr. 2000;130(7): 1865S–1867S. PMID:10867064.7. 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:17241913.8. 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:10198297.9. 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:15539275.10. 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:20368372.11. 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. 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:21367943.13. 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:21795443.14. Tarnopolsky, MA, et al. Evaluation of protein requirements for strength trained athletes. J Appl Physiol; 1992;73:1986-1995.15. Colgan M. The Anti-inflammatory Athlete. Sound Concepts: Indian Fork, UT, 2012.16. Lemon P et al. Protein requirements and muscle mass/strength changes during intensive exercise in novice bodybuilders. J Appl Physiol, 1992;73:767-775.17. Kreider RB, Campbell B. Protein for exercise and recovery. Phys Sportsmed. 2009 Jun;37(2):13-21. doi: 10.3810/psm.2009.06.1705.18. Areta J.L., Burke, L.M., Camera, D.M., West, D.W., Crawshay, S., Moore, D.R., et al. Reduced resting skeletal muscle protein synthesis is rescued by resistance exercise and protein ingestions following short-term energy deficit. Am. J. Physiol. Endocrinol. Metab. 2014,306(8): E989–E997. doi:10.1152/ajpendo. 00590.2013. PMID:24595305.19. Areta, J.L., Burke, L.M., Ross, M.L., Camera, D.M., West, D.W., Broad, E.M., et al. Timing and distribution of protein ingestion during prolonged recovery from resistance exercise alters myofibrillar protein synthesis. J. Physiol. 2013,591(9): 2319–2331. doi:10.1113/jphysiol.2012.244897. PMID:234

1 comment:

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