[Purification of dopamine-beta-monooxygenase and extremely acidic, copper-containing proteins from the adrenal medulla. Extremely acidic, copper-containing proteins as electron donors for dopamine-beta-monooxygenase].

A procedure for purification of two copper-containing proteins from bovine adrenal medulla has been developed. The method is based on the extraction of proteins with Triton X-100, DEAE-cellulose chromatography and fractionation with polyethylene glycol. The yield of dopamine-beta-monooxygenase and extremely acidic copper-containing protein per 1 kg of brain medullar tissue is 100 and 150 mg, correspondingly. The ability of the reduced extremely acidic copper-containing protein to act as an electron donor in the reactions of side chain hydroxylation of tyramine and dopamine catalyzed by dopamine-beta-monooxygenase was demonstrated. The kinetics of the products formation and oxygen consumption in the course of these reactions and the specific activities of dopamine-beta-monooxygenase were compared, using the reduced extremely acidic copper-containing protein, ascorbate and ferrocyanide as cosubstrates.