Purification and properties of glutamate synthase from Thiobacillus thioparus.
Glutamate synthase was purified about 250-fold from Thiobacillus thioparus and was characterized. The molecular weight was estimated as 280,000 g/mol. The enzyme showed absorption maxima at 280, 380, and 450 nm and was inhibited by Atebrin, suggesting that T. thioparus glutamate synthase is a flavop...
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| Publicado no: | J Bacteriol |
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| Principais autores: | , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
American Society for Microbiology (ASM)
1977
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC235071/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/14919/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.129.3.1173-1182.1977 |
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