Purification and properties of the 5,10-methenyltetrahydromethanopterin cyclohydrolase from Methanobacterium thermoautotrophicum.

The 5,10-methenyltetrahydromethanopterin cyclohydrolase of Methanobacterium thermoautotrophicum was purified 128-fold to homogeneity. The enzyme had a subunit Mr of 41,000 as indicated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. From high-performance size exclusion chromatography o...

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Bibliographic Details

Published in:	J Bacteriol
Main Authors:	DiMarco, A A, Donnelly, M I, Wolfe, R S
Format:	Artigo
Language:	Inglês
Published:	American Society for Microbiology (ASM) 1986
Subjects:	Research Article
Online Access:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC213648/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/3782039/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.168.3.1372-1377.1986
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