Membranes of chromaffin granules. Isolation and partial characterization of two proteins.
Membranes of chromaffin granules were isolated from the adrenal glands of four different species. The solubilized membrane proteins could be resolved into several bands by polyacrylamide-gel electrophoresis (alkaline and acid gel systems). Two major protein components appeared to be common to the chromaffin granule membranes of ox, horse, pig and man. The various membrane proteins of bovine chromaffin granules were separated by filtration on Sephadex G-200 in the presence of sodium dodecyl sulphate. Two major membrane proteins (A and B) were obtained in purified form. Treatment of protein A with 2-mercaptoethanol before electrophoresis resulted in two more rapidly migrating subunits, whereas protein B was unaffected by mercaptoethanol treatment. The amino acid compositions of the two purified proteins were determined. They are very similar to that of the total membrane proteins but significantly different from that of the chromogranins, the soluble proteins of chromaffin granules.
D000313:Adrenal Medulla / Q000032:analysis*; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D002458:Cell Fractionation; D002499:Centrifugation, Density Gradient; D002845:Chromatography; D003594:Cytoplasmic Granules / Q000032:analysis*; D004589:Electrophoresis, Disc; D006736:Horses; D006801:Humans; D008566:Membranes / Q000032:analysis* / Q000201:enzymology; D008623:Mercaptoethanol; D011506:Proteins / Q000302:isolation & purification*; D013552:Swine
D000596:Amino Acids; D011506:Proteins; D008623:Mercaptoethanol