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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Detaylı Bibliyografya
Asıl Yazarlar: te Brömmelstroet, B W, Hensgens, C M, Geerts, W J, Keltjens, J T, van der Drift, C, Vogels, G D
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: 1990
Konular:
Research Article
Online Erişim:https://ncbi.nlm.nih.gov/pmc/articles/PMC208478/
https://ncbi.nlm.nih.gov/pubmed/2298699
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