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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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Sonraí Bibleagrafaíochta
Main Authors: Schirch, V, Hopkins, S, Villar, E, Angelaccio, S
Formáid: Artigo
Teanga:Inglês
Foilsithe: 1985
Ábhair:
Rochtain Ar Líne:https://ncbi.nlm.nih.gov/pmc/articles/PMC219072/
https://ncbi.nlm.nih.gov/pubmed/3891721
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