doi: 10.1016/0005-2736(76)90441-7.
A water-soluble Mg2+-ATPase from erythrocyte membranes
- PMID: 133717
- DOI: 10.1016/0005-2736(76)90441-7
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A water-soluble Mg2+-ATPase from erythrocyte membranes
Biochim Biophys Acta.
.
Abstract
A ouabain-insensitive ATPase activity associated with the water-soluble proteins of the human and bovine erythrocyte membrane is demonstrated by means of activity-staining in polyacrylamide gels. The ATPase activity from both sources had an absolute requirement for Mg2+, activity becoming easily detectable at 0.2 mM Mg2+. At low Mg2+ concentrations added Ca2+ appeared to decrease the intensity of the ATPase stain. The activity is unaffected by monovalent cations, does not hydrolyse p-nitrophenyl phosphate and is not inhibited by 2 : 4 dinitrophenol. The ATPase has an apparent molecular weight of approximately 100 000 as determined by electrophoresis in acrylamide gels containing dodecyl sulphate.
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