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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Detalhes bibliográficos

Publicado no:	J Bacteriol
Principais autores:	Schirch, V, Hopkins, S, Villar, E, Angelaccio, S
Formato:	Artigo
Idioma:	Inglês
Publicado em:	American Society for Microbiology (ASM) 1985
Assuntos:	Research Article
Acesso em linha:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC219072/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/3891721/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.163.1.1-7.1985
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