The "branched chain" amino acids (BCAA's), leucine, isoleucine and valine are so called because the side chains of these amino acids (the part of the molecule that differentiates the amino acids) are made up of non-linear (branching) carbon chains. The BCAA's are essential amino acids, meaning that they must be consumed in the diet (rather than manufactured in the body) and constitute a more than one third of the amino acid composition of skeletal muscle(1). During high intensity exercise, the BCAA's are oxidized for use as fuel and to maintain oxidative metabolite concentration(2). Supplementing with BCAA's reduces exercise-induced muscle proteolysis (breakdown)(3) and also stimulates muscle protein synthesis(4). Daily BCAA supplementation may also reduce muscle damage, promote strength recovery and even enhance blood oxygen carrying capacity(5).
Of the three BCAA's, leucine plays a special role in skeletal muscle metabolism, in particular by exerting an anti-catabolic and anabolic effect on protein metabolism(6-10). Leucine metabolites that have been sold as sports (HMB) or animal feed supplements (keto-isocaproate) also exert anabolic effects in humans and growing animals(11, 12). In fact, leucine incorporation into skeletal muscle has long been used as a marker of muscle protein synthesis(13) and oxidation(14). Because leucine so powerfully stimulates muscle protein synthesis, some researchers have suggested L-Leucine supplementation to combat age-associated loss of skeletal muscle mass (sarcopenia)(9).
True Nutrition offers each of the BCAA's independently or pre-mixed, which is specifically designed with a 2:1:1 ratio favoring leucine, for the reasons listed above. True Nutrition's BCAA Boost also contains this ratio of BCAA's with other ingredients designed to promote fat loss and spare muscle mass when dieting. BCAA's can be blended in a post-workout supplement (10+ grams) to maximize muscle anabolism (along with supplements such as creatine, L-Glutamine, Waxy Maize, and / or a protein powder blend), or taken during training or between meals to reduce protein breakdown (e.g., during a low calorie diet).
As a dietary supplement, take 1 Serving 1-3 times per day.
L-Leucine, L-Isoleucine, L-Valine, Soy Lecithin (Less than 1%).
If you are currently pregnant or nursing, consult a physician prior to use. Keep out of the reach of children.
Although this product may not contain one or all of the following, this product is manufactured in a facility that handles milk, soy, egg, peanut, nut, tree, fish, crustaceans/shellfish, and wheat products.
Use the table below to approximate the gram equivalent weight for a given level measuring spoon (US Standard). Please note that accurate dosing should only be done with a recommended calibrated scale.
|Measuring Spoon (level) ||g ||mg |
|90cc Scoop ||30.5 ||30511 |
|70cc Scoop ||23.7 ||23731 |
|29.6cc Scoop ||10.0 ||10035 |
|25cc Scoop ||8.5 ||8475 |
|Tablespoon ||5.0 ||5014 |
|10cc Scoop ||3.4 ||3390 |
|½ Tablespoon ||2.5 ||2507 |
|Teaspoon ||1.7 ||1671 |
|½ Teaspoon ||0.8 ||836 |
|1.7cc Scoop ||0.6 ||576 |
|¼ Teaspoon ||0.4 ||418 |
|1/8 Teaspoon ||0.2 ||209 |
|1/16 Teaspoon ||0.1 ||104 |
|1/32 Teaspoon ||0.1 ||52 |
DISCLAIMER: The above description is provided for information only and does not constitute medical advice. Please consult your physician or the appropriately licensed professional before engaging in a program of exercise or nutritional supplementation. No information in this site has been reviewed by the FDA. No product is intended to treat, diagnose, or cure any disease.
1. Harper, A.E., et al., Branched-chain amino acid metabolism. Annu Rev Nutr, 1984. 4: p. 409-54. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=6380539
2. Gibala, M.J., Regulation of skeletal muscle amino acid metabolism during exercise. Int J Sport Nutr Exerc Metab, 2001. 11(1): p. 87-108. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=11255139
3. Tang, F.C., Influence of branched-chain amino acid supplementation on urinary protein metabolite concentrations after swimming. J Am Coll Nutr, 2006. 25(3): p. 188-94. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16766776
4. Shimomura, Y., et al., Exercise promotes BCAA catabolism: effects of BCAA supplementation on skeletal muscle during exercise. J Nutr, 2004. 134(6 Suppl): p. 1583S-1587S. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15173434
5. Ohtani, M., et al., Amino acid mixture improves training efficiency in athletes. J Nutr, 2006. 136(2): p. 538S-543S. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16424143
6. Goldberg, A.L., Protein synthesis during work-induced growth of skeletal muscle. J Cell Biol, 1968. 36: p. 653-658.
7. Goldberg, A.L. and H.M. Goodman, Amino acid transport during work-induced growth of skeletal muscle. Am J Physiol, 1969. 216: p. 1111-1115.
8. Goldberg, A.L., et al., Mechanism of work-induced hypertrophy of skeletal muscle. Med Sci.Sports, 1975. 7: p. 185-198.
9. Fujita, S. and E. Volpi, Amino acids and muscle loss with aging. J Nutr, 2006. 136(1 Suppl): p. 277S-80S. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16365098
10. Kimball, S.R. and L.S. Jefferson, Signaling pathways and molecular mechanisms through which branched-chain amino acids mediate translational control of protein synthesis. J Nutr, 2006. 136(1 Suppl): p. 227S-31S. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16365087
11. Flakoll, P.J., et al., Influence of alpha-ketoisocaproate on lamb growth, feed conversion, and carcass composition. J Anim Sci, 1991. 69(4): p. 1461-7.
12. Nissen, S., et al., Effect of leucine metabolite beta-hydroxy-beta-methylbutyrate on muscle metabolism during resistance-exercise training. J. Appl. Physiol., 1996. 81(5): p. 2095-104.
13. Nair, K.S., et al., Leucine incorporation into mixed skeletal muscle protein in humans. Am J Physiol, 1988. 254(2 Pt 1): p. E208-13. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=3279803
14. Boirie, Y., et al., Slow and fast dietary proteins differently modulate postprandial protein accretion. Proc Natl Acad Sci U S A, 1997. 94(26): p. 14930-5. http://www.ncbi.nlm.nih.gov/cgi-bin/Entrez/referer?http://www.pnas.org/cgi/content/full/94/26/14930