NDLI: Chemical modification of Glu-953 of the alpha chain of Na+,K(+)-ATPase associated with inactivation of cation occlusion.

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Chemical modification of Glu-953 of the alpha chain of Na+,K(+)-ATPase associated with inactivation of cation occlusion.

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Chemical modification of Glu-953 of the alpha chain of Na+,K(+)-ATPase associated with inactivation of cation occlusion.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Goldshleger, R. Tal, D. M. Stein, W. D. Karlish, S. J. Moorman, J.
Description	Author Affiliation: Goldshleger R ( Biochemistry Department, Weizmann Institute of Science, Rehovot, Israel.);
Abstract	We have investigated the role, number, and identity of glutamate (or aspartate) residues involved in cation occlusion on Na+, K(+)-ATPase, using the carboxyl reagent N,N'-dicyclohexylcarbodiimide (DCCD). Extensive use is made of selectively trypsinized Na+,K(+)-ATPase--the so-called '19-kDa membranes'--containing a 19-kDa COOH-terminal, smaller (8-11 kDa) membrane-embedded fragments of the alpha chain, and a largely intact beta chain; these membranes have normal Rb+ and Na+ occlusion capacities. The 19-kDa peptide and a smaller (approximately 9 kDa) unidentified peptide(s) are labeled by [14C]DCCD in a Rb(+)-protectable fashion. Rb(+)-protected [14C]DCCD incorporation into the '19 kDa membranes' and into native Na+,K(+)-ATPase is linearly correlated with inactivation of Rb+ occlusion. Similar linear correlations are observed when Rb(+)-protected [14C]DCCD incorporation is measured by examination of labeling of 19-kDa peptide purified from '19-kDa membranes' or of alpha chain purified from native enzyme. Stoichiometries, estimated by extrapolation, are as follows: (for '19-kDa membranes') close to one DCCD per Rb+ site and one DCCD per 19-kDa peptide; and (for native enzyme) close to two DCCD per phosphoenzyme and two DCCD per alpha chain. We suggest that each of two K+ (or Na+) sites contains a carboxyl group, one located in the 19-kDa peptide and one elsewhere in the alpha chain. After cyanogen bromide digestion of purified, labeled alpha chain, or of 19-kDa peptide, a labeled fragment of apparent M(r) approximately 4 kDa was detected and was identified as that with NH2-terminal Lys-943. Rb(+)-protected [14C]DCCD incorporation was associated almost exclusively with Glu-953. We suggest that the cation occlusion 'cage' consists of ligating groups donated by different trans-membrane segments and includes two carboxyl groups such as Glu-953 (and perhaps Glu-327) as well as neutral groups, in two K+ (or Na+) sites, but only neutral groups in the third Na+ site.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	15
Volume Number	89
Language	English
Publisher	National Academy of Sciences
Publisher Date	1992-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Dicyclohexylcarbodiimide Pharmacology Glutamates Sodium-Potassium-Exchanging ATPase Antagonists & Inhibitors Amino Acid Sequence Animals Binding Sites Chromatography, Gel Cyanogen Bromide Glutamic Acid Kidney Enzymology Kinetics Macromolecular Substances Molecular Sequence Data Peptide Fragments Isolation & Purification Peptide Mapping Rubidium Sequence Homology, Nucleic Acid Swine Trypsin Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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