RT Journal Article SR Electronic T1 Mechanism of Secretion from the Adrenal Medulla JF Molecular Pharmacology JO Mol Pharmacol FD American Society for Pharmacology and Experimental Therapeutics SP 81 OP 89 VO 3 IS 1 A1 HARVEY J. SAGE A1 W. J. SMITH A1 N. KIRSHNER YR 1967 UL http://molpharm.aspetjournals.org/content/3/1/81.abstract AB Rabbit antisera have been prepared against a protein contained within the catecholamine storage vesicles of cow adrenal glands. Although the vesicle protein appeared homogeneous by physical and chemical criteria, immunologic analysis showed the presence of small amounts of highly immunogenic contaminants representing less than 1% of the total protein. The major contaminant was shown to be dopamine-β-oxidase, and antibodies to this contaminant could be removed from the antisera by absorption with a dopamine-β-oxidase-containing fraction obtained from a DEAE-cellulose fractionation of a crude catecholamine storage vesicle lysate. The resultant purified antivesicle protein sera were used to measure the release of the vesicle protein during stimulation of isolated perfused adrenal glands. It was found that catecholamines and vesicle protein appeared in the perfusates in ratios very similar to that present in the whole gland.