STUDY ON HUMAN ERYTHROCYTE MEMBRANE Na~+-K~+-ATPasc 1. ACTIVITY DETERMINATION AND SOME BIOCHEMICAL CHARATERISTICS
- VernacularTitle:人红细胞膜Na~+-K~+-ATP酶的研究——Ⅰ.活力测定及某些生化特性
- Author:
Jianxin LI
- Publication Type:Journal Article
- From:
Academic Journal of Second Military Medical University
1981;0(04):-
- CountryChina
- Language:Chinese
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Abstract:
Human erythrocyte membrane preparation was obtained by washing after hy-potonic hemolysis and repeating ultracentrifugal sedimentation. The activity of Na+-K+-ATPase were 6.15 nmol P/min/mg protein.Ouabain used as a specific inhibitor in Na+-K+-ATPase assay could be replaced by omitting Na + and K+ in the original assay medium.The Km of ATP for Na+-K+-ATPase increased with the elevation of tempe-rat ure from 27 C to 37 C and the activation energy of ATP hydrolysis for membrane Na+-K+-ATPase was measured being 1.8?104 cal/mol.Membrane Na+-K+-ATPase activity was not significantly influenced by addition of Co2+, Ni2+, Cd2+, Zn2+, Pb2+ into assay medium,while Sn2+ had an inhibition effect on concentration of 10-4M. Mn2+ stimulated the membrane total ATPase and Mg2+-ATPase activities, having an antagonist property to ouabine effect.Hence Mn2+ disturbed Na+-K+-ATPase activity determintion.No effects of some bile acids on membrane Na+-K + -ATPase activities were observed.