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Molecular Pharmacology, Vol 3, 81-89, Copyright © 1967 by the American Society for Pharmacology and Experimental Therapeutics
1 Departments of Biochemistry and Pathology, Duke University Medical Center,
Durham, North Carolina 27706
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-
-oxidase, and antibodies to this contaminant could be removed from the antisera by absorption with a
dopamine-
-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.