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A kinetic and binding study of the reactivity of Escherichia coli ATPase to N-ethoxycarbonyl-2-ethoxy-1,2-dihydroquinoline.

作者信息

Satre M, Dupuis A, Bof M, Vignais P V

出版信息

Biochem Biophys Res Commun. 1983 Jul 29;114(2):684-9. doi: 10.1016/0006-291x(83)90835-5.

DOI:10.1016/0006-291x(83)90835-5
PMID:6224490
Abstract

Escherichia coli H+-ATPase (ECF1) was inactivated in a time- and concentration-dependent manner by N-ethoxycarbonyl-2-ethoxy-1,2-dihydroquinoline (EEDQ), a selective carboxyl group reagent. Among the subunits of ECF1, only the beta subunit was modified by EEDQ. The reaction of 1 mol of EEDQ per mol of ECF1 resulted in total inactivation, in spite of the fact that the enzyme possesses three beta subunits.

摘要

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引用本文的文献

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Recent developments on structural and functional aspects of the F1 sector of H+-linked ATPases.H⁺ 连接的ATP酶F1 部分结构和功能方面的最新进展。
Mol Cell Biochem. 1984;60(1):33-71. doi: 10.1007/BF00226299.