Glycoproteins of the chromaffin-granule matrix: use of lectin blotting to distinguish several separate classes.
The soluble proteins released by hypotonic lysis of highly purified bovine adrenal chromaffin granules were analysed by one- and two-dimensional electrophoresis, followed by transfer to nitrocellulose and decoration with lectins or specific antibodies. The effects of neuraminidase treatment, and of chemical deglycosylation by trifluoromethanesulphonic acid, were investigated. It was shown that lectins could be used to distinguish the two major series of chromogranins from each other, from dopamine beta-hydroxylase and from several minor, unidentified glycoprotein components of the lysate. Antibody decoration revealed a complex series of peptides containing enkephalin sequences, some of which changed their electrophoretic mobility on treatment with trifluoromethanesulphonic acid.
D000313:Adrenal Medulla / Q000032:analysis* / Q000648:ultrastructure; D000818:Animals; D002417:Cattle; D002837:Chromaffin Granules / Q000032:analysis*; D002838:Chromaffin System / Q000032:analysis*; D002845:Chromatography; D002864:Chromogranins / Q000032:analysis; D004299:Dopamine beta-Hydroxylase / Q000032:analysis; D006023:Glycoproteins / Q000032:analysis*; D037102:Lectins
D002864:Chromogranins; D006023:Glycoproteins; D037102:Lectins; D004299:Dopamine beta-Hydroxylase