Purification and properties of 5,10-methenyltetrahydromethanopterin cyclohydrolase from Methanosarcina barkeri.
The 5,10-methenyltetrahydromethanopterin cyclohydrolase from Methanosarcina barkeri was purified 313-fold to a specific activity of 470 mumol min-1 mg-1 at 37 degrees C and pH 7.8. At this stage, the enzyme was pure as judged from polyacrylamide gel electrophoresis. The monofunctional enzyme was oxy...
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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)
1990
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC208478/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/2298699/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.172.2.564-571.1990 |
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