Isolated p65 protein reproduces membrane binding activity of synaptic vesicles.
Neuroreport
; 3(2): 177-80, 1992 Feb.
Article
em En
| MEDLINE
| ID: mdl-1623168
ABSTRACT
Purified synaptic vesicles are highly enriched with a protein which binds cell plasma membranes. The binding is selective for acidic phospholipids and sialoglycosphingolipids. In partition chromatography of vesicle proteins, the binding activity was co-eluted with a limited set of proteins. Among them the most abundant species were two vesicle-specific proteins p65 and synaptophysin. In affinity chromatography of vesicle proteins, only p65 bound to a column of immobilized lysoganglioside. The same protein, purified by preparative electrophoresis, retained the binding activity and fully reproduced the hemagglutinating property and the selectivity for acidic lipids of whole vesicles. The results suggest that the (hemagglutinating) lipid binding properties of the vesicles are mainly if not exclusively due to p65.
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Base de dados:
MEDLINE
Assunto principal:
Fosfolipídeos
/
Esfingolipídeos
/
Vesículas Sinápticas
/
Proteínas de Ligação ao Cálcio
/
Glicoproteínas de Membrana
/
Proteínas do Tecido Nervoso
Limite:
Humans
Idioma:
En
Ano de publicação:
1992
Tipo de documento:
Article