文章基本信息

标题：Topological organization of proteins in an intracellular secretory organelle: the synaptic vesicle
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作者：J A Wagner ; R B Kelly
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1979
卷号：76
期号：8
页码：4126-4130
DOI：10.1073/pnas.76.8.4126
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Intact synaptic vesicles prepared from the electric organ of the marine elasmobranch Narcine brasiliensis have eight major polypeptides demonstrable on sodium dodecyl sulfate gels. Six of these copurify with the synaptic vesicles during isolation of vesicles by chromatography on CPG-3000 and, by this criterion, are specific to vesicles. The other two are either shared by many membrane or are contaminants. One of these proteins comigrates with actin. Three different approaches were used to determine which proteins were exposed on the external, cytoplasmic surface of the vesicle and which were internal. The first was susceptibility to the proteases trypsin, Streptomyces griseus protease, and Pronase; the second was labeling by the membrane-impermeable reagent diazotized [125I]iodosulfanilic acid; and the third was iodination catalyzed by lactoperoxidase. In general, the three approaches give the same result: six of the eight proteins are on the external, cytoplasmic surface and two are accessible only after the vesicles are lysed by freezing and thawing or by detergents. Five of the vesicle-specific proteins are external and one is internal. The actin-like protein is internal. Proteins involved in the interaction of vesicles with the presynaptic membrane during exocytosis might be expected to be vesicle specific and external.