Serine hydroxymethyltransferase from Escherichia coli: purification and properties.

Serine hydroxymethyltransferase from Escherichia coli was purified to homogeneity. The enzyme was a homodimer of identical subunits with a molecular weight of 95,000. The amino acid sequence of the amino and carboxy-terminal ends and the amino acid composition of cysteine-containing tryptic peptides...

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Библиографические подробности
Главные авторы: Schirch, V, Hopkins, S, Villar, E, Angelaccio, S
Формат: Artigo
Язык:Inglês
Опубликовано: 1985
Предметы:
Research Article
Online-ссылка:https://ncbi.nlm.nih.gov/pmc/articles/PMC219072/
https://ncbi.nlm.nih.gov/pubmed/3891721
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