Purification and properties of gamma-glutamyltranspeptidase from Proteus mirabilis.
gamma-Glutamyltranspeptidase was purified ca. 15,200-fold from cell-free extracts of Proteus mirabilis to electrophoretic homogeneity and then crystallized. The enzyme has an estimated molecular weight of 80,000 and consists of two different subunits with molecular weights of ca. 47,000 and 28,000....
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| Pubblicato in: | J Bacteriol |
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| Autori principali: | , , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
American Society for Microbiology (ASM)
1984
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC214722/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/6148333/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.160.1.341-346.1984 |
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