Purification of a protein inhibitor of erythrocyte plasma membrane Ca(2+)-ATPase by Ca(2+)-ATPase-sepharose affinity chromatography.
A protein inhibitor of erythrocyte plasma membrane Ca(2+)-ATPase was purified to homogeneity using a Ca(2+)-ATPase-Sepharose affinity column. Inhibitor isolated by anion exchange chromatography was loaded onto the affinity column in the presence of Ca2+ and the purified inhibitor was eluted with EGTA. The estimated yield was 0.1-0.2 mg protein inhibitor/1. red cells. SDS-polyacrylamide gel electrophoresis of freshly purified inhibitor revealed one single silver stained band with an apparent molecular mass of 50-51 kD.
Au
K S
KS
Department of Biochemistry, University of Hong Kong, Hong Kong.
D000818:Animals; D000252:Calcium-Transporting ATPases / Q000037:antagonists & inhibitors*; D002462:Cell Membrane / Q000737:chemistry*; D002846:Chromatography, Affinity / Q000379:methods*; D004791:Enzyme Inhibitors / Q000302:isolation & purification*; D004910:Erythrocyte Membrane / Q000737:chemistry*
D004791:Enzyme Inhibitors; D000252:Calcium-Transporting ATPases