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CaMBP-10介导的质膜H~(+)-ATP酶磷酸化对该酶活性的调节

摘要

CaMBP-10在活体处理条件下,抑制IAA诱导的质膜H~(+)-ATP酶活性及其磷酸化,抑制作用可被IAA逆转并在外加CaM时被消除,与前期BP-10对IAA生理应答的调节效应相吻合。并且在各项处理中,质膜H~(+)-ATP酶活性与其磷酸化水平呈现极显著的正相关。

关键词： 钙调素; 钙调素结合蛋白; 生长素; 质膜H~(+)-ATP酶; 蛋白磷酸化

The regulation of CaM BP-10 mediated PM H~(+)-ATPase activity by phosphorylation

Abstract

The present study showed that BP-10 inhibited the IAA-induced activity and phosphorylation of plasma membrane H~(+)-ATPase (PM H~(+)-ATPase) in in vivo experiment. The inhibitory effect can be reversed by IAA and can also be overcome by the addition of CaM. The results are perfectly in accord with those of our preliminary studies. The activity of PM-ATPase (Y) has been found to be positively correlated with the extent of its phosphorylation (X) which can be expressed as Y=22.3303+0.7656X(P<0.01).

Key words: Calmodulin;Calmodulin binding protein auxin;Plasma membrane H~(+)-ATPase; Protein phosphorylation;

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引用本文：

. CaMBP-10介导的质膜H~(+)-ATP酶磷酸化对该酶活性的调节[J]. 生理学报 1998; 50 (3): .

. The regulation of CaM BP-10 mediated PM H~(+)-ATPase activity by phosphorylation. Acta Physiol Sin 1998; 50 (3): (in Chinese with English abstract).