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Subcellular Site of Biosynthesis of the Catecholamine Biosynthetic Enzymes in Bovine Adrenal Medulla
Author(s) -
Sabban Esther L.,
Goldstein Menek
Publication year - 1984
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1984.tb06093.x
Subject(s) - polysome , biosynthesis , phenylethanolamine , biochemistry , tyrosine hydroxylase , phenylethanolamine n methyltransferase , adrenal medulla , enzyme , biology , tyrosine , antiserum , subcellular localization , catecholamine , microbiology and biotechnology , chemistry , cytoplasm , antibody , gene , rna , ribosome , endocrinology , immunology
The subcellular site of biosynthesis of the catecholamine biosynthetic enzymes was examined. Free and membrane‐bound polysomes were prepared from bovine adrenal medulla and mRNA was isolated from these polysomes. Both were active in directing cell‐free translations. Immunoprecipitation of cell‐free products with specific antisera localized the biosynthesis of the subunits of tyrosine hydroxylase (TH) (apparent M r = 61,000) and of phenylethanolamine N ‐methyltransferase (PNMT) (apparent M r = 32,000) on free polysomes, compared with biosynthesis of subunits of dopamine β‐hydroxylase (DBH) (apparent M r = 67,000) on membrane‐bound polysomes. Cross‐reactivity between translation products was observed. Antibodies for DBH recognized a poly‐peptide with electrophoretic mobility identical to newly synthesized PNMT. However increasing concentrations of antibodies to DBH recognized at most 1/2 of the PNMT formed. The results of this study show the subcellular distribution of the catecholamine synthesizing enzymes is determined by their site of biosynthesis.