Purification and characterization of a molybdenum-pterin-binding protein (Mop) in Clostridium pasteurianum W5.
A large-scale fractionation scheme purified the major molybdenum(Mo)-binding protein (Mop) from crude extracts of Clostridium pasteurianum, with a 10 and 0.2% yield of Mo and protein, respectively. The apparent molecular weight of the purified molybdoprotein is 5,700, as determined by sodium dodecyl...
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| Vydáno v: | J Bacteriol |
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| Hlavní autoři: | , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
American Society for Microbiology (ASM)
1986
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC213536/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/3782020/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.168.2.688-693.1986 |
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