Purification and properties of methyl coenzyme M methylreductase from acetate-grown Methanosarcina thermophila.

Methyl coenzyme M methylreductase from acetate-grown Methanosarcina thermophila TM-1 was purified 16-fold from a cell extract to apparent homogeneity as determined by native polyacrylamide gel electrophoresis. Ninety-four percent of the methylreductase activity was recovered in the soluble fraction...

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Vydáno v:	J Bacteriol
Hlavní autoři:	Jablonski, P E, Ferry, J G
Médium:	Artigo
Jazyk:	Inglês
Vydáno:	American Society for Microbiology (ASM) 1991
Témata:	Research Article
On-line přístup:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC207811/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/2013570/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.173.8.2481-2487.1991
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