Примеры использования Tryptophan на Английском языке и их переводы на Русский язык
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Two trivial enzymatic steps from tryptophan.
Well, tryptophan is an amino acid and it's everywhere.
This enzyme participates in tryptophan metabolism.
When tryptophan is disintegrated its fluorescence diminishes.
With specific amino acids such as lysine and tryptophan.
Tryptophan is not synthesized by the body, and comes with food.
Gentamicin sulphate and the zinc-tryptophan coordination compound.
Tryptophan and vitamins are destroyed by the acid treatment.
The trp operon is active only when cellular tryptophan is scarce.
Tryptophan is one of the first amino acids that have been classified as essential.
It is also recommended eating foods rich in vitamin B and tryptophan.
In short tryptophan acts as a corepressor for its own biosynthesis.
Nicotinic acid can be synthesized from tryptophan or aspartic acid.
Tryptophan, an essential amino acid is a precursor for the synthesis of serotonin.
One example of such compound is aromatic amino acid tryptophan.
On the other hand,block of tryptophan uptake by the cells may prevent aging.
It is a synthetic dipeptide,which consists of amino acid fragments- glutamine and tryptophan.
To help in the essential amion acid tryptophan is converted to nicotinic acid;
Secondly, tryptophan has to compete with other amino acids for entry into the brain.
This occurred because zein lacks the essential amino acids lysine and tryptophan.
Dependence of fluorescence on tryptophan concentration was measured for this purpose.
Tryptophan helps to maintain mental health, positive mood and cognitive functions.
Write, please, what is the amino acid tryptophan, and the products it contains.
Unfortunately, tryptophan faces many obstacles during his journey in brain tissue.
For most of them, the first synthesis step is decarboxylation of tryptophan to form tryptamine.
Tryptophan and methionine oxidation are posttranslational modifications of the crystallin polypeptide.
One of the genes regulated by trp repressor, trpR,codes for the tryptophan repressor protein itself.
The decrease of tryptophan fluorescence after the exposure to different sources of active particles has been investigated.
Members of the IRF family are characterized by a conserved N-terminal DNA-binding domain containing tryptophan(W) repeats.
The concentration of-SH-groups in tryptophan, albumin, and methemoglobin increases when exposed to plasma radiation.