Примери коришћења Leucine на Енглеском и њихови преводи на Српски
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Leucine Reduce hypoglycemic symptoms.
Today it is known that toxicare leucine, isoleucine, valine, methionine.
Leucine- This BCAA is used for bulking.
And when we're talking about regenerating muscle,the key is protein higher in leucine,” he says.
Leucine, which has a general strengthening effect on the human immunity;
The characteristic smell of urine is associated with the presence of a substance produced from leucine.
Leucine and isoleucine content in products(in grams per 100 g of product), respectively.
Furthermore, BCAAs, specifically leucine, plays a direct role in initiating muscle protein synthesis.
Leucine also slightly lowers the level of sugar in blood and stimulates growth hormone release.
Red meat is also a good source of leucine, an amino acid that helps build muscle.
Basic Leucine zipper domain(bZIP domain): is found in many DNA-binding eukaryotic proteins.
The molecular formula C6H13NO2 may refer to:Aminocaproic acid Isoleucine Leucine β-Leucine Norleucine.
Until you get enough leucine, protein synthesis won't run at 100%,” Layman explains.
The optimal ratio for the three BCAAs in the diet and supplements is 2: 1:1(two parts of leucine, a part of isoleucine and a part of valine).
In addition, eggs contain leucine(responds by cell division) and other amino acids that our hair needs.
These essential amino acids can be found in common foods(for example, there is a lot of leucine in cheese), as well as in special additives.
Leucine is an essential amino acid that interacts with valine and isoleucine to promote the healing of bones, muscles and skin.
They are full of protein,vitamins and minerals(leucine among them) that are required by the body to complete the work and recovery after exercise.
Leucine zippers are present in both eukaryotic and prokaryotic regulatory proteins, but are mainly a feature of eukaryotes.
One part of the domain contains a region that mediates sequence specific DNA binding properties and the leucine zipper that is required to hold together(dimerize) two DNA binding regions.
As we indicated before, leucine is an essential amino acid that we have to contribute to our body through diet, being unable to synthesize it.
The amino acid composition also changes, the amount of histidine, tryptophan, aspartic acid, phenylalanine,tyrosine increases and the amount of leucine, arginine, alanine, glycine, proline is reduced.
Along with isoleucine and valine, leucine is one of the most abundant essential amino acids of branched chain, which become the only ones used during physical exercise by our body.
In 1999, Layman conducted experiments on rats andfound that a specific amount of the essential amino acid leucine, contained in all protein, is necessary to kick-start synthesis.
Due to the high content of branched-chain amino acids(BCAA,~26%),especially leucine, alpha-lactalbumin effectively supports and stimulates muscle protein synthesis, making it the ideal protein source for improving muscle health and help prevent sarcopenia during ageing.
This enzyme catalyses the following chemical reaction Release of a variety of N-terminal residues(especially glutamate and leucine) from peptides, provided tryptophan(or at least phenylalanine or tyrosine) is the penultimate residue.
Amongst peptide and small-molecule substrates, the most consistently reported specificity is for small,hydrophobic amino acids(e.g. leucine, valine and isoleucine) at the P2 position, and large hydrophobic amino acids(e.g. phenylalanine and tyrosine) at the P1 position.