INHIBITION OF (NA+ + K+)-ATPASE BY OUABAIN - INVOLVEMENT OF CALCIUM AND MEMBRANE-PROTEINS

被引:34
作者
LELIEVRE, L
ZACHOWSKI, A
CHARLEMAGNE, D
LAGET, P
PARAF, A
机构
[1] INRA,CNRS,VIROL & IMMUNOL STN,EQUIPE RECH 802,F-78850 THIVERVAL GRIGNON,FRANCE
[2] FAC MED ANGERS,BIOPHYS LAB,F-49000 ANGERS,FRANCE
关键词
(Murine plasmocytoma); (Na<sup>+</sup> + K<sup>+</sup>)-ATPase; Ca<sup>2+</sup> dependence; Chelating agent; Ouabain sensitivity;
D O I
10.1016/0005-2736(79)90338-9
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 [生物化学与分子生物学]; 081704 [应用化学];
摘要
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. © 1979.
引用
收藏
页码:399 / 408
页数:10
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