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Identification and Characterization of the Major Proteins of Mammalian Brain Synaptic Vesicles
Author(s) -
Floor E.,
Leeman S. E.
Publication year - 1988
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1988.tb03049.x
Subject(s) - synaptic vesicle , identification (biology) , neuroscience , vesicle , chemistry , computational biology , biology , biochemistry , membrane , botany
Highly purified rat and cow brain synaptic vesicles contain major proteins with molecular weights of ∼74,000, 60,000, 57,000, 40,000, 38,000, and 34,000 by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis. The presence of the major proteins on synaptic vesicles was confirmed by immunoprecipitation of intact rat brain synaptic vesicles with a synaptic vesicle‐specific monoclonal antibody. The 40,000‐M r protein appeared to be identical to the 38,000‐M r integral membrane glycoprotein, p38 or synaptophysin, previously identified as a major component of mammalian synaptic vesicles. The isoelectric point of the 75,000‐M r proteins from either rat or cow brain synaptic vesicles is 5.0, and the pI of the 57,000‐M r protein is ∼5.1 in both species. The similarity in size and charge of several major proteins in rat and cow synaptic vesicles suggests a high degree of structure conservation of these proteins in diverse mammalian species and raises the possibility that a set of functions common to most or all mammalian synaptic vesicles is mediated by these proteins.