Purification and characterization of an oxygen-labile, NAD-dependent alcohol dehydrogenase from Desulfovibrio gigas.

A NAD-dependent, oxygen-labile alcohol dehydrogenase was purified from Desulfovibrio gigas. It was decameric, with subunits of M(r) 43,000. The best substrates were ethanol (Km, 0.15 mM) and 1-propanol (Km, 0.28 mM). N-terminal amino acid sequence analysis showed that the enzyme belongs to the same...

Celý popis

Uloženo v:
Podrobná bibliografie
Hlavní autoři: Hensgens, C M, Vonck, J, Van Beeumen, J, van Bruggen, E F, Hansen, T A
Médium: Artigo
Jazyk:Inglês
Vydáno: 1993
Témata:
Research Article
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC204602/
https://ncbi.nlm.nih.gov/pubmed/8491707
Tagy: Přidat tag
Žádné tagy, Buďte první, kdo otaguje tento záznam!

Podobné jednotky