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...
محفوظ في:
| الحاوية / القاعدة: | J Bacteriol |
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| المؤلفون الرئيسيون: | , , , |
| التنسيق: | Artigo |
| اللغة: | Inglês |
| منشور في: |
American Society for Microbiology (ASM)
1985
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| الموضوعات: | |
| الوصول للمادة أونلاين: | 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 |
| الوسوم: |
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