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Ca2+-stimulated Mg2+-dependent ATPase (Ca2+ + Mg2+-ATPase) stimulated by calmodulin, by partial proteolysis or by oleic acid in erythrocyte membranes was inhibited by various derivatives of the naturally occurring alkaloid berbamine. The ability of these derivatives to inhibit trypsin-activated Ca2+ + Mg2+-ATPase correlated well with their ability to inhibit the calmodulin-stimulated enzyme. Inhibition of the trypsin-activated Ca2+ + Mg2+-ATPase by O-4-(ethoxybutyl)berbamine (EBB) was competitive with respect to ATP. The Ki for inhibition was about 8 microM. These results suggest that the binding site of EBB on the activated Ca2+ + Mg2+-ATPase may bear structural similarity to that on calmodulin, and may be closely related to the ATP-binding site on the enzyme.
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February 1982,
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Y H Xu, and
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March 1977,
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Y H Xu, and
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May 1980,
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Y H Xu, and
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March 1981,
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Y H Xu, and
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October 1975,
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Y H Xu, and
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January 1973,
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Y H Xu, and
J Liu, and
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January 1974,
Ukrains'kyi biokhimichnyi zhurnal,
Y H Xu, and
J Liu, and
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November 1987,
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Y H Xu, and
J Liu, and
S P Zhang, and
L H Liu
July 1981,
Biochimica et biophysica acta,
Y H Xu, and
J Liu, and
S P Zhang, and
L H Liu
February 1981,
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