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Molecular Pharmacology, Vol 7, 569-580, Copyright © 1971 by the American Society for Pharmacology and Experimental Therapeutics

Isolation and Characterization of a Tyrosine Hydroxylase Cofactor from Bovine Adrenal Medulla

TOM LLOYD 1 and NORMAN WEINER 1

1 Departments of Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, and University of Colorado School of Medicine, Denver, Colorado 80220

Tyrosine hydroxylase pterin cofactor has been isolated from bovine adrenal medulla tissue by means of column chromatography on Florisil and Dowex 50-H+ columns, and paper chromatography in several solvent systems. The cofactor has been identified as a 6-substituted, unconjugated pteridine by permanganate oxidation to pterin-6-carboxylic acid. Its paper chromatographic behavior and fluorescence spectrum are identical with those of biopterin. The concentration of this pterin in bovine adrenal medulla tissue is estimated to be approximately 10 nmoles/g of tissue. The low concentration of this cofactor in chromaffin tissue emphasizes its importance in the regulation of tyrosine hydroxylase activity and the potential susceptibility of the enzyme system to end product feedback inhibition by catecholamines, which, according to Nagatsu, Levitt, and Udenfriend [J. Biol. Chem. 239, 2910 (l964)], appear to antagonize the action of the cofactor competitively in this hydroxylation reaction.

Submitted on April 16, 1971




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