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

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.

authors

Satre M,Dupuis A,Bof M,Vignais PV

doi

10.1016/0006-291x(83)90835-5

subject

Has Abstract

pub_date

1983-07-29 00:00:00

pages

684-9

issue

2

eissn

0006-291X

issn

1090-2104

pii

0006-291X(83)90835-5

journal_volume

114

pub_type

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