Relationships between Erythrocyte Membrane Phosphorylation and Adenosine Triphosphate Hydrolysis

摘要: Abstract Human erythrocyte membranes were incubated with a low concentration of terminally labeled ATP the aim detecting phosphorylated intermediate adenosine triphosphatase activity. A large portion material briefly at 37° turned over and had properties consistent participation in sodium ion-stimulated ATPase activity, including following: (a) magnesium ions present, addition stimulated an increase both 32P bound to trichloracetic acid-precipitated membrane rate hydrolysis. (b) The Na+-activated correlated quantitatively amount sensitive hydroxylamine, agreement other preparations. (c) Addition potassium breakdown presence ions. At 0°, was hydroxylamine. Its turnover apparent upon excess or ADP, but not guanosine triphosphate, deoxyguanosine diphosphate, AMP, 3-phosphoglycerate. ethylenediamine tetraacetate allowed dephosphorylation proceed, it shown that approximate similar Although activity 2 µm concentration, manifestations altered sensitivity 0° have been attributed temperature-induced changes conformation catalytic sites. relationship (14C)ADP-ATP exchange investigated. It found least 30% associated which could be separated from hydrolytic after incubation ATP. This did appear related activities tested, nucleoside diphosphokinase, adenylate kinase, phosphoglycerate kinase.