RT Journal Article
SR Electronic
T1 Purification and Properties of Dopamine β-Hydroxylase from Human Pheochromocytoma
JF Molecular Pharmacology
JO Mol Pharmacol
FD American Society for Pharmacology and Experimental Therapeutics
SP 1009
OP 1015
VO 10
IS 6
A1 RICHARD A. STONE
A1 NORMAN KIRSHNER
A1 JACQUELINE REYNOLDS
A1 THOMAS C. VANAMAN
YR 1974
UL http://molpharm.aspetjournals.org/content/10/6/1009.abstract
AB Dopamine β-hydroxylase (EC 1.14.17.1) was isolated as a pure protein from a human pheochromocytoma. The tumor enzyme has chemical and physical properties similar to those of the enzyme isolated from bovine adrenal medulla. Both enzymes are glycoproteins and have similar amino acid compositions. Both enzymes have subunit molecular weights of 75,000-77,000 determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis and by equilibrium centrifugation in 6 M guanidine hydrochloride after reduction and carboxymethylation. Equilibrium centrifugation in the presence of 6 M guanidine hydrochloride in the absence of reducing agents gives subunit molecular weights of about 150,000 for both enzymes. Studies of the native enzyme obtained from the human tumor show that, in contrast to the bovine enzyme, human dopamine β-hydroxylase has an unusual tendency to dissociate and aggregate; however, its behavior on Sephadex G-200 suggests a molecular weight of 300,000, the same as that of the bovine enzyme. ACKNOWLEDGMENTS The authors are grateful to Drs. Sam Wells and William Peete for their help in obtaining the tissue used for this investigation.