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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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| Main Authors: | , , , |
|---|---|
| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
1985
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| Fag: | |
| Online adgang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC219072/ https://ncbi.nlm.nih.gov/pubmed/3891721 |
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