Demonstration and partial characterization of glutathione disulfide-stimulated ATPase activity in the plasma membrane fraction from rat hepatocytes.
作者： P Nicotera , M Moore , G Bellomo , F Mirabelli , S Orrenius
DOI: 10.1016/S0021-9258(18)89502-3
关键词: ATPase 、 Low affinity 、 ATP hydrolysis 、 Intracellular 、 Chemistry 、 Biochemistry 、 Glutathione disulfide 、 Atpase activity 、 Membrane fraction 、 Cell biology 、 Molecular biology
摘要: A highly purified plasma membrane fraction isolated from rat hepatocytes was found to catalyze the hydrolysis of ATP in response micromolar concentrations glutathione disulfide (GSSG). This process exhibited distinct kinetic parameters suggesting existence both a high and low affinity component. The apparent Km values (GSSG) for were 140 microM 1 mM components, respectively. Disulfides other than GSSG also stimulate hydrolysis. similarity between properties GSSG-stimulated ATPase those reported transport erythrocytes (Kondo, T., Dale, G. L., Beutler, E. (1980) Proc. Natl. Acad. Sci. U.S.A. 77, 6359-6362) suggests that may function active extrusion intracellular GSSG.
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