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Inhibition of (Na+ + K+)-ATPase by ouabain: involvement of calcium and membrane proteins.

作者信息

Lelievre L, Zachowski A, Charlemagne D, Laget P, Paraf A

出版信息

Biochim Biophys Acta. 1979 Nov 2;557(2):399-408. doi: 10.1016/0005-2736(79)90338-9.

DOI:10.1016/0005-2736(79)90338-9
PMID:227455
Abstract

Treatment of plasma membrane isolated from murine plasmocytoma MOPC 173 with an EDTA-containing buffer resulted in a 300-fold increase in sensitivity of (Na+ + K+)-stimulated Mg2+-ATPase to ouabain. This phenomenon was associated with the solubilization by EDTA of phospholipid free proteins (approx. 30 000-34 000 daltons) from the cytoplasmic face of the plasma membrane and with removal of about 90% of the membrane bound Ca2+. The recovery of the original resistance to ouabain required specifically Ca2+ and was associated with a binding of the solubilized proteins to the membrane.

摘要

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1
Inhibition of (Na+ + K+)-ATPase by ouabain: involvement of calcium and membrane proteins.
Biochim Biophys Acta. 1979 Nov 2;557(2):399-408. doi: 10.1016/0005-2736(79)90338-9.
2
[Purification of a membrane protein modifying the sensitivity of Na+/K+ ATPase to ouabain from a supernatant of plasma membrane treated with EDTA].[从经乙二胺四乙酸(EDTA)处理的质膜上清液中纯化一种可改变钠钾ATP酶对哇巴因敏感性的膜蛋白]
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C R Seances Acad Sci D. 1979 Dec 10;289(15):1137-40.
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Roles of proteins from inner face of plasma membranes in susceptibility of of (Na+ + K+)-stimulated Mg2+ adenosinetriphosphatase to ouabain.质膜内表面蛋白质在(钠 + 钾)刺激的镁 - 腺苷三磷酸酶对哇巴因敏感性中的作用。
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Biochim Biophys Acta. 1976 Dec 2;455(2):277-86. doi: 10.1016/0005-2736(76)90304-7.

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