Organization of thiol groups of electric-eel electric-organ sodium-plus-potassium ion-stimulated adenosine triphosphatase studied with bifunctional reagents
- 1 March 1980
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 185 (3) , 787-790
- https://doi.org/10.1042/bj1850787
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.This publication has 13 references indexed in Scilit:
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