A water-extractable Ca2+-atpase from erythrocyte membranes.
The Ca2+- and Mg2+-stimulated ATPase activities present in low ionic strength extracts of erythrocyte membranes have been separated from each other. The Ca2+-ATPase appears to be associated with particulate meterial which could be sedimented by high-speed centrifugation. The pellet obtained was composed mainly of components 1, 2, 4.5, 5 and 7. A soluble protein from the band 3 region, known to be responsible for the Mg2+-ATPase activity, was not detected in this pellet.
D000251:Adenosine Triphosphatases / Q000097:blood / Q000302:isolation & purification; D017301:Ca(2+) Mg(2+)-ATPase; D000252:Calcium-Transporting ATPases / Q000097:blood* / Q000302:isolation & purification; D004910:Erythrocyte Membrane / Q000201:enzymology*; D004912:Erythrocytes / Q000201:enzymology*; D006801:Humans; D012995:Solubility; D014867:Water
D014867:Water; D000251:Adenosine Triphosphatases; D017301:Ca(2+) Mg(2+)-ATPase; D000252:Calcium-Transporting ATPases