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.