突触前α -干酪毒素受体组分与突触囊泡膜蛋白p65相互作用。

Biomedical science Pub Date : 1991-01-01
I N Surkova, E V Grishin
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引用次数: 0

摘要

牛脑α -脑毒素受体的纯化制剂含有39 kDa和65 kDa的蛋白。序列分析表明,65kda蛋白与p65相对应,p65是一种先前在大鼠突触囊泡中发现的突触囊泡膜蛋白,而39kda蛋白是65kda蛋白的蛋白水解片段。39 kDa和65 kDa蛋白出现在受体样品中,因为它们与α -latrotoxin受体的组分具有特异性相互作用。这种相互作用可能代表了突触囊泡膜与突触前末端质膜的灌注和/或融合的重要步骤,这两者都是神经递质胞吐的最后步骤。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Presynaptic alpha-latrotoxin receptor components interact with protein p65 of synaptic vesicle membranes.

Purified preparations of bovine brain alpha-latrotoxin receptor contain proteins of 39 kDa and 65 kDa. Sequence analysis shows that the 65 kDa protein corresponds to p65, a synaptic vesicle membrane protein previously identified in rat synaptic vesicles, and that the 39 kDa protein is a proteolytic fragment of the 65 kDa protein. The 39 kDa and 65 kDa proteins appear in receptor samples because of their specific interaction with components of the alpha-latrotoxin receptor. This interaction may represent an essential step in perfusion and/or the fusion of synaptic vesicle membranes with the plasma membrane of the presynaptic terminal, both of which are final steps in the exocytosis of neurotransmitters.

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