Organization of Thiol Groups of Electric-eel Electric-organ Sodium-plus-potassium Ion-stimulated Adenosine Triphosphatase Studied with Bifunctional Reagents

Overview

Journal Biochem J

Specialty Biochemistry

Date 1980 Mar 1

PMID 6248037

Citations 2

Authors

W E Harris

W L Stahl

Affiliations

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Abstract

The reactions of three bifunctional thiol-blocking reagents of differing cross-linking spans and two monofunctional thiol-blocking reagents with the Na+ + K+-stimulated ATPase of the electric-eel electric organ were examined. 1,5-Difluoro-2,4-dinitrobenzene with a cross-linking span of 0.3--0.5 nm (3--5 A) and high solubility in non-polar solvent was the most efficient inhibitor of enzyme activity; thus essential thiol groups exist in a non-polar environment and are approx. 0.3--0.5 nm (3--5 A) from their nearest thiol-group neighbours. Ligands promoting phosphorylation of the Na+ + K+-stimulated ATPase decreased the number of thiol groups bridged by 1,5-difluoro-2,4-dinitrobenzene and by 4,4'-difluoro-3,3'-dinitrodiphenyl sulphone [0.7--1.0 nm (7--10 A) span]. Phosphorylation is associated with a conformational change in the enzyme.

Citing Articles

Phosphorylation states of the (Na+ + K+)-transporting ATPase in preparations from lamb kidney and electric-eel (Electophorus electricus) electric organ.

Harris W, Stahl W Biochem J. 1984; 218(2):341-5.

PMID: 6324756 PMC: 1153346. DOI: 10.1042/bj2180341.

Conformational states of the (Na+ + K+)-transporting ATPase. Formation of 240 000-Mr and 116 000-Mr polypeptides in the presence of a bifunctional thiol probe.

Harris W, Stahl W Biochem J. 1984; 218(2):331-9.

PMID: 6324755 PMC: 1153345. DOI: 10.1042/bj2180331.

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