Surkova I N, Grishin E V
Shemyakin Institute of Biorganic Chemistry, Academy of Sciences of the USSR, Moscow.
Biomed Sci. 1991;2(4):417-20.
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.
纯化的牛脑α-拉毒素受体制剂含有39 kDa和65 kDa的蛋白质。序列分析表明,65 kDa的蛋白质对应于p65,一种先前在大鼠突触小泡中鉴定出的突触小泡膜蛋白,而39 kDa的蛋白质是65 kDa蛋白质的蛋白水解片段。39 kDa和65 kDa的蛋白质出现在受体样品中是因为它们与α-拉毒素受体的成分发生特异性相互作用。这种相互作用可能是灌注和/或突触小泡膜与突触前终末质膜融合的关键步骤,这两个步骤都是神经递质胞吐作用的最终步骤。