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从专性厌氧细菌巴氏芽孢梭菌中部分纯化对二环己基碳二亚胺敏感的膜三磷酸腺苷酶复合物。

Partial purification of a dicyclohexylcarbodi-imide-sensitive membrane adenosine triphosphatase complex from the obligately anaerobic bacterium Clostridium Pasteurianum.

作者信息

Clarke D J, Morris J G

出版信息

Biochem J. 1976 Mar 15;154(3):725-9. doi: 10.1042/bj1540725.

Abstract

The membrane adenosine triphosphatase complex of vegetatively growing Clostridium pasteurianum, solublized with Triton X-100, has been recovered as a significantly purified particulate preparation that is still sensitive to inhibition by dicyclohexylcarbodiimide and butyricin 7423.

摘要

用Triton X-100溶解的巴氏芽孢梭菌营养生长阶段的膜腺苷三磷酸酶复合物,已被回收为一种显著纯化的颗粒制剂,该制剂仍对二环己基碳二亚胺和丁酸菌素7423的抑制敏感。

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本文引用的文献

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Membrane-bound adenosinetriphosphatase of Escherichia coli. II. Physicochemical properties of the enzyme.
J Biochem. 1974 Dec;76(6):1175-82. doi: 10.1093/oxfordjournals.jbchem.a130670.
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Membrane-associated ATPase activity from Micrococcus lysodeikticus.
Biochim Biophys Acta. 1968 Apr 29;150(3):531-3. doi: 10.1016/0005-2736(68)90156-9.

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