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阴离子两亲分子的多聚体模拟钙调蛋白对环核苷酸磷酸二酯酶的刺激作用。

Multimers of anionic amphiphiles mimic calmodulin stimulation of cyclic nucleotide phosphodiesterase.

作者信息

Gietzen K, Xü Y H, Galla H J, Bader H

出版信息

Biochem J. 1982 Dec 1;207(3):637-40. doi: 10.1042/bj2070637.

Abstract

Oleic acid, phosphatidylserine and pyrenedecanoic acid were found to activate calmodulin-deficient cyclic nucleotide phosphodiesterase at concentrations above their critical micellar concentration. In contrast with calmodulin these activators do not require the presence of Ca2+ for their action. It is shown that the size of phosphatidylserine vesicles is of crucial importance with respect to the activating potency of phosphatidylserine. Fluorescence measurements with the probe pyrenedecanoic acid revealed that micelles rather than monomers are the active species for stimulation of phosphodiesterase. There are indications that this result also may be applied to the other activators.

摘要

油酸、磷脂酰丝氨酸和癸二酸芘在浓度高于其临界胶束浓度时能激活钙调蛋白缺陷型环核苷酸磷酸二酯酶。与钙调蛋白不同,这些激活剂发挥作用时不需要Ca2+的存在。研究表明,磷脂酰丝氨酸囊泡的大小对于磷脂酰丝氨酸的激活效力至关重要。用探针癸二酸芘进行的荧光测量表明,胶束而非单体是刺激磷酸二酯酶的活性物质。有迹象表明,这一结果也可能适用于其他激活剂。

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