Isolation of carbon monoxide dehydrogenase from Acetobacterium woodii and comparison of its properties with those of the Clostridium thermoaceticum enzyme.

An oxygen-labile carbon monoxide dehydrogenase was purified to at least 98% homogeneity from fructose-grown cells of Acetobacterium woodii. Gel filtration and electrophoresis experiments gave molecular weights of 480,000 and 153,000, respectively, of the active enzyme. The molecular weights for the...

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Hlavní autoři: Ragsdale, S W, Ljungdahl, L G, DerVartanian, D V
Médium: Artigo
Jazyk:Inglês
Vydáno: 1983
Témata:
Research Article
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC217820/
https://ncbi.nlm.nih.gov/pubmed/6309745
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