Purification of the nickel protein carbon monoxide dehydrogenase of Clostridium thermoaceticum

FEBS Letters

Ritter, Maria¹  Diekert, Gabriele¹ 

[1] Fachbereich Biologie/Mikrobiologie, Philipps-Universität, Lahnberge, D-3550 Marburg/Lahn, FRG

关键词: Carbon monoxide dehydrogenase;    Acetogenic bacteria;    Clostridium thermoaceticum Nickel enzyme;   

DOI  :  10.1016/0014-5793(83)80338-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The carbon monoxide dehydrogenase was purified from Clostridium thermoaceticum to apparent homogeneity. The 120-fold purified enzyme with app. M _r 250000 had a nickel content of 10 ± 2 μmol Ni/protein.

【 授权许可】

Unknown