SYNAPHIN - A PROTEIN ASSOCIATED WITH THE DOCKING/FUSION COMPLEX IN PRESYNAPTIC TERMINALS
SYNAPHIN - A PROTEIN ASSOCIATED WITH THE DOCKING/FUSION COMPLEX IN PRESYNAPTIC TERMINALS
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DOI：
10.1006/bbrc.1995.2241
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发表时间：
1995-08-24
影响因子：
3.1
通讯作者：
ABE, T
中科院分区：
文献类型：
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作者：
ISHIZUKA, T;SAISU, H;ABE, T
我们先前发现了一个与参与神经递质释放的对接/融合复合体相关的19 kDa蛋白质。根据该蛋白的部分氨基酸序列，用寡核苷酸探针从牛脑cDNA文库中克隆了该蛋白的cDNA。该基因编码的蛋白质(命名为突触素)是一种富含谷氨酸和赖氨酸残基的亲水性蛋白质。它缺乏任何假定的跨膜片段或强疏水结构域。用抗突触素抗体的免疫印迹法在脑组织中只检测到神经系统中的蛋白，它主要存在于可溶部分，在突触小泡中很少。(C)1995年学术出版社。
We previously identified a 19 kDa protein associated with the docking/fusion complex involved in neurotransmitter release. A cDNA for this protein was cloned from a bovine brain cDNA library using an oligonucleotide probe based on its partial amino acid sequence. The protein (named synaphin) en coded by the cDNA is a very hydrophilic protein rich in glutamic acid and lysine residues. It lacks any putative transmembrane segments or strongly hydrophobic domains. Immunoblots with antibodies against synaphin detected the protein only in the nervous system among the tissues examined In brain, it exists mainly in the soluble fraction and is scarce in synaptic vesicles. (C) 1995 Academic Press, Inc.