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PMID: 6447513 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Inhibition of red cell Ca2+-ATPase by vanadate.

Biochimica et biophysica acta ·Vol. 600 ·No. 3 ·1980-08-14 ·Pages 781-90

Bond GH, Hudgins PM

Abstract

1. The Mg2+- plus Ca2+-dependent ATPase (Ca2+-ATPase) in human red cell membranes is susceptible to inhibition by low concentrations of vanadate. 2. Several natural activators of Ca2+-ATPase (Mg2+, K+, Na+ and calmodulin) modify inhibition by increasing the apparent affinity of the enzyme for vanadate. 3. Among the ligands tests, K+, in combination with Mg2+, had the most pronounced effect on inhibition by vanadate. 4. Under conditions optimal for inhibition of Ca2+-ATPase, the K 1/2 for vanadate was 1.5 microM and inhibition was nearly complete at saturating vanadate concentrations. 5. There are similarities between the kinetics of inhibition of red cell Ca2+-ATPase and (Na+ + K+)-ATPase prepared from a variety of sources; however, (Na+ + K+)-ATPase is approx. 3 times more sensitive to inhibition by vanadate.

MeSH Terms
Calcium-Transporting ATPases/antagonists & inhibitors,blood Erythrocyte Membrane/enzymology Erythrocytes/enzymology Humans Kinetics Magnesium/pharmacology Potassium/pharmacology Sodium/pharmacology Vanadates Vanadium/pharmacology
Chemicals
Vanadium Vanadates Sodium Calcium-Transporting ATPases Magnesium Potassium
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Bond G H
Hudgins P M
Article Info
Journal
Biochimica et biophysica acta
Abbr.
Biochim Biophys Acta
ISSN
0006-3002
Published
1980-08-14
Pages
781-90
Language
English
Region
Netherlands
NLM ID
0217513
Subset
IM
Grants
NIADDK NIH HHS · AM 19162 · United States
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