Should you be drinking BCAA’s?
AMINO ACIDS IN GENERAL
Muscles can not grow without protein and despite their variety; all proteins are composed of just 20 different amino acids. Proteins are macromolecules constructed from long strings of units called amino acids. Amino acids are the building blocks of proteins. Each amino acid has an amino group (NH3) on one end, a carboxyl acid group on the other, and a C-H group in the middle. Differences in the charge and structure of the amino acids affect the shape and functions of the proteins constructed from them.
The eight that the body cannot produce, which are isoleuceine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine, are called essential amino acids because they must be ingested in food or supplementation. Two more that the body can make are histidine and arginine, which are sometimes considered essential in children because their rapidly growing bodies cannot synthesize them fast enough.
WHAT ARE THE FUNCTIONS OF BCAA’S?
BCAA’s act as nitrogen carriers which assist the muscles in synthesizing other aminos needed for anabolic muscle action. In simpler terms, it is a combining of simpler aminos to form a complex whole muscle tissue Therefore, BCAA’s stimulate production of insulin, the main function of which is to allow circulating blood sugar to be taken up by the muscle cells and used as a source of energy. This insulin production promotes amino acid uptake by the muscle. BCAA’s are both anabolic and anti-catabolic because of their ability to significantly increase protein synthesis, facilitate the release of hormones such as growth hormone (GH), IGF-1, and insulin, and help maintain a favorable testosterone to cortisol ratio.
BCAA’s are also excellent anti-catabolic because they can help prevent protein breakdown and muscle loss, which is significantly important to those who are pre-contest diets. During these times of low caloric intake, the use of BCAA is strongly recommended because there is a greater risk of muscle loss due to a decrease in the rate of protein synthesis and an increase of proteolysis, which is the hydrolytic breakdown of proteins into simpler, soluble substances such as peptides and amino acids, as occurs during digestion.
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