Properties of the HCO-3-stimulated Mg2+ -ATPase activity in red cell membranes.
The HCO-3-stimulated Mg2+ -ATPase activity in red cell ghost fragments was investigated. Increasing the HCO-3 concentration in the incubation medium resulted in increased ATPase activity. NaHCO3 appeared to be more effective than KHCO3 in this regard. The ATPase activities were slightly stimulated by increases in ionic strength and utilized ITP almost as readily as ATP. A Mg/ATP ratio of 1.0 and a pH of 7.6 yielded maximum activity. These properties are of interest since the present enzyme is the only unquestionable instance where a HCO-3 ATPase is located in the surface membrane of a cell.
D000251:Adenosine Triphosphatases / Q000097:blood*; D000818:Animals; D001639:Bicarbonates / Q000494:pharmacology*; D002712:Chlorides / Q000097:blood; D004789:Enzyme Activation; D004910:Erythrocyte Membrane / Q000201:enzymology*; D004912:Erythrocytes / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D008274:Magnesium / Q000097:blood; D008297:Male; D009994:Osmolar Concentration; D011817:Rabbits
D001639:Bicarbonates; D002712:Chlorides; D000251:Adenosine Triphosphatases; D008274:Magnesium