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磷蛋白B - 50的突触前定位

Presynaptic localization of phosphoprotein B-50.

作者信息

Sorensen R G, Kleine L P, Mahler H R

出版信息

Brain Res Bull. 1981 Jul;7(1):57-61. doi: 10.1016/0361-9230(81)90098-8.

Abstract

A major phosphoprotein of synaptic membranes, the phosphorylation of which is stimulated by Ca2+ and inhibited by ACTh, appears to be identical with protein B-50 described by Zwiers, Schotman and Gispen [40]. We have investigated its subsynaptic localization by means of a variety of subfractionation techniques and compared it with that of a number of other phosphoproteins found in synaptic membranes. It appears to be predominantly, if not exclusively, associated with presynaptic membranes of low bouyant density. This localization pattern is similar to, but somewhat more extreme than that exhibited by Protein I, as a brain specific phosphoprotein studied by Greengard and his collaborators [11].

摘要

一种突触膜的主要磷蛋白,其磷酸化受Ca2+刺激并被促肾上腺皮质激素抑制,似乎与Zwiers、Schotman和Gispen [40]描述的蛋白B - 50相同。我们通过多种亚分级分离技术研究了其突触下定位,并将其与突触膜中发现的其他一些磷蛋白的定位进行了比较。它似乎主要(如果不是唯一的话)与低浮力密度的突触前膜相关。这种定位模式与Greengard及其合作者[11]研究的一种脑特异性磷蛋白蛋白I所表现出的模式相似,但更为极端。

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