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Differential glycosylatin 에 의한 dopamine beta - hydroxylase 의 multiple Forms 의 생산
황온유,조동협 ( On Yon Hwang,Tong Hyub Joh ) 생화학분자생물학회 1991 BMB Reports Vol.24 No.2
The enzyme dopamie beta-hydroxylase (DBH) catalyzes the conversion of dopamine to norepinephrine. DBH is a glycoprotein present in the catecholamine-containing vesicles and exists in both membrane-bound and soluble forms. We have previously shown that the soluble form of bovine adrenal medullary DBH have multiple forms of 75, 72 and 69 kDa as determined by SDS-PAGE We sought to investigate the relationship between glycosylation and the different molecular weight forms of bovine soluble DBH. Comparison of molecular weights of deglycosylated and glycosylated DBH revealed that after removal of the carbohydrate moieties, the triplet of 75, 72, and 69 kDa DBH became a single band of 66 kDa on SDS-PAGE, indicating that these multiple forms originated from differential glycosylation. This was further supported by the fact that DBH translated in vitro and thus without post translational processing mechanisms was a single band of 67 kDa, 1 kDa larger than the delycosylated mature DBH due to the presence of the cleavable N-terminal signal peptide. Comparison of the activites of the glycosylated and deglycosylated DBH revealed that carbohydrate moieties do not directly contribute to the catalytic activity of the mature DBH.
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