Mixability Taste Home Page Store Front Alanine is a crystalline, free-form amino acid. The liver can convert L-alanine into glucose as needed for muscle fuel; when glycogen stores are low, it can convert the glucose into glycogen. Glycogen is a storage form of glucose.   Aside from its role in protein synthesis, alanine is second only to glutamine in prominence as a circulating amino acid. In this capacity it serves a unique role in the transfer of nitrogen from peripheral tissue to the liver. Alanine is transferred to the circulation by many tissues, but mainly by muscle, in which alanine is formed from pyruvate at a rate proportional to intracellular pyruvate levels. Liver accumulates plasma alanine, reverses the transamination that occurs in muscle, and proportionately increases urea production. The pyruvate is either oxidized or converted to glucose via gluconeogenesis. When alanine transfer from muscle to liver is coupled with glucose transport from liver back to muscle, the process is known as the glucose-alanine cycle. The key feature of the cycle is that in 1 molecule, alanine, peripheral tissue exports pyruvate and ammonia (which are potentially rate-limiting for metabolism) to the liver, where the carbon skeleton is recycled and most nitrogen eliminated.   There are 2 main pathways to production of muscle alanine: directly from protein degradation, and via the transamination of pyruvate by alanine transaminase, ALT (also referred to as serum glutamate-pyruvate transaminase, SGPT). The glucose-alanine cycle is used primarily as a mechanism for skeletal muscle to eliminate nitrogen while replenishing its energy supply. Glucose oxidation produces pyruvate which can undergo transamination to alanine. This reaction is catalyzed by alanine transaminase, ALT (ALT used to be called serum glutamate-pyruvate transaminase, SGPT). Additionally, during periods of fasting, skeletal muscle protein is degraded for the energy value of the amino acid carbons and alanine is a major amino acid in protein. The alanine then enters the blood stream and is transported to the liver. Within the liver alanine is converted back to pyruvate which is then a source of carbon atoms for gluconeogenesis. The newly formed glucose can then enter the blood for delivery back to the muscle. The amino group transported from the muscle to the liver in the form of alanine is converted to urea in the urea cycle and excreted. Primarily L-Alanine spares other Amino acids from being cannibalized much like L-Glutamine does but from a different pathway. What is most importantly spared is BCAA’s. This leaves essential amino acids such as these to do their primary job of building muscle tissue. Don’t think that your body won’t opt for cannibalizing amino acids if you are taking in carbs. Yes carbs will spare protein breakdown but under intense enough resistance exercise and definitely under more aerobic exercise your body may very well step into the realm of gluconeogenesis for energy production. Some argue that L-Glutamine doesn't pass the intestines beyond the splanchnic bed into the blood pool. And it's those individuals that claim L-Alanine is better than L-Glutamine. But that doesn't relay into the fact that L-Glutamine is ineffective. L-Glutamine is effective in that L-Glutamine when needed for gluconeogenesis supplies glucose differently than does L-Alanine. L-Alanine releases glucose from the liver and L-Glutamine does so from the kidneys. And since both L-Glutamine and L-Alanine are the most abundant amino acids in muscle tissue and the blood pool. Both are on stand by and are the first aminos to just to the occasion to be synthesized keeping other essential aminos from being cannibalized.

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