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...
Zapisane w:
| Wydane w: | J Bacteriol |
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| Główni autorzy: | , , , |
| Format: | Artigo |
| Język: | Inglês |
| Wydane: |
American Society for Microbiology (ASM)
1985
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| Hasła przedmiotowe: | |
| Dostęp online: | 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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