Properties of partially purified bovine brain dopamine beta-hydroxylase.
Dopamine beta-hydroxylase has been partially purified from bovine brain. A 140-fold purification factor was achieved using solubilization with Triton X-100, ammonium sulphate fractionation between 20-50 per cent saturation, affinity chromatography on concanavalin A-Sepharose 4 B and then filtration through Sephadex G200. The specific activity at the end was 51 nmoles/h/mg protein. The majority of endogenous inhibitors were lost. Immunological studies, kinetic studies, studies on the interaction with lectins and the effect of carboxylic acids on enzyme activity were carried out. Our data are in favour of the close similarity between the bovine brain and adrenal enzymes. No major differences could be found, at least with the characterization experiments using in the present study.
D000311:Adrenal Glands / Q000201:enzymology; D000818:Animals; D001921:Brain / Q000201:enzymology*; D002264:Carboxylic Acids / Q000494:pharmacology; D002417:Cattle; D002951:Citrates / Q000494:pharmacology; D003208:Concanavalin A / Q000494:pharmacology; D003300:Copper / Q000494:pharmacology; D004299:Dopamine beta-Hydroxylase / Q000276:immunology / Q000302:isolation & purification / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D012276:Ricin / Q000494:pharmacology
D002264:Carboxylic Acids; D002951:Citrates; D003208:Concanavalin A; D003300:Copper; D012276:Ricin; D004299:Dopamine beta-Hydroxylase