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1
Adavaces in Gene Theraphy for Brain Diseases

Joh, Tong hyub Korean Society of Molecular Biology 1994 Molecules and cells Vol.4 No.1
- 복사/대출신청
2
STRUCTURAL ANALYSIS OF THE SOLUBLE FORM OF BOVINE DOPAMINE BETA-HYDROXYLASE

Hwang, On-You,Joh, Tong-Hyub The Korean Society of Toxicology Korea Environment 1990 Toxicological Research Vol.6 No.1
- 원문보기
Dopamine beta-hydroxylase (DBH) is a neurotransmitter biosynthetic enzyme which catalyzes the conversion of dopamine to norepinephrine. Although structural studies of the mature form of this enzyme have been extensive, the culmination of these finding had been hightly controversial and contradictory. In this study, biochemical approaches were taken to characterize the structure of mature DBH. Soluble bovine DBH was purified from aderenal medulla. Three bands of 69 kDa, 72 kDa and 75 kDa which were physically separable and similar in structure were observed by SDS-PAGE. Furthermore, gas phase sequence analysis revealed that the 72 kDa band consists of two polypeptides which are present at equimolar concentrations and differed in that one had three extra amino acids at the N-terminus. Taken together, the soluble form of DBH exist in at least four forms, three identified by SDS-PAGE, one of which consists of two polypeptides as identified by N-terminal sequence analysis. The significance of these forms and their possible biosynthetic mechanisms are discussed.
3
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
- 원문보기
- 복사/대출신청
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.