小檗胺衍生物对红细胞膜中活化的钙刺激镁依赖性ATP酶的作用。
The effect of berbamine derivatives on activated Ca2+-stimulated Mg2+-dependent ATPase in erythrocyte membranes.
作者信息
Xu Y H, Liu J, Zhang S P, Liu L H
机构信息
Institute for Molecular Biology, Nankai University, Tianjin, People's Republic of China.
出版信息
Biochem J. 1987 Dec 15;248(3):985-8. doi: 10.1042/bj2480985.
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.
钙调蛋白、部分蛋白水解或油酸刺激红细胞膜中的钙刺激镁依赖性ATP酶（Ca2+ + Mg2+-ATP酶）会受到天然生物碱小檗胺各种衍生物的抑制。这些衍生物抑制胰蛋白酶激活的Ca2+ + Mg2+-ATP酶的能力与其抑制钙调蛋白刺激的酶的能力密切相关。O-4-（乙氧基丁基）小檗胺（EBB）对胰蛋白酶激活的Ca2+ + Mg2+-ATP酶的抑制作用对ATP而言具有竞争性。抑制常数Ki约为8微摩尔。这些结果表明，EBB在激活的Ca2+ + Mg2+-ATP酶上的结合位点可能与在钙调蛋白上的结合位点具有结构相似性，并且可能与该酶上的ATP结合位点密切相关。
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