SYNAPHIN - A PROTEIN ASSOCIATED WITH THE DOCKING/FUSION COMPLEX IN PRESYNAPTIC TERMINALS

被引：82

作者：

ISHIZUKA, T

SAISU, H

ODANI, S

ABE, T

机构：

[1] NIIGATA UNIV,BRAIN RES INST,DEPT CELLULAR NEUROBIOL,NIIGATA 951,JAPAN

[2] NIIGATA UNIV,FAC SCI,DEPT BIOL,NIIGATA 951,JAPAN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1995年 / 213卷 / 03期

关键词：

D O I：

10.1006/bbrc.1995.2241

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：1107 / 1114

页数：8

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