Abstract
Dopamine-β-hydroxylase (EC 1.14.2.1) has been isolated as a pure protein from bovine-adrenal glands. Although the molecular weight of the native protein is well established (290,000), sodium dodecyl sulfate-gel electrophoresis under dissociating conditions gave a single band with a molecular weight of about 75,000. The enzyme contains about 4% carbohydrate, which consists of residues of mannose, glucosamine, galactose, glucose, fucose, and sialic acid. The pure enzyme also contains about 4 atoms of copper per molecule. It is concluded that dopamine-β-hydroxylase is a tetrameric glycoprotein.
Keywords: sodium dodecyl sulfate-gel electrophoresis, molecular weight, transmission of nerve impulses
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- Axelrod J. Dopamine- -hydroxylase: regulation of its synthesis and release from nerve terminals. Pharmacol Rev. 1972 Jun;24(2):233–243. [PubMed] [Google Scholar]
- Belpaire F., Laduron P. Tissue fractionation and catecholamines. 3. Intracellular distribution of endogenous inhibitors of dopamine- -hydroxylase in adrenal medulla. Biochem Pharmacol. 1970 Apr;19(4):1323–1331. doi: 10.1016/0006-2952(70)90047-x. [DOI] [PubMed] [Google Scholar]
- CLARKE J. T. SIMPLIFIED "DISC" (POLYACRYLAMIDE GEL) ELECTROPHORESIS. Ann N Y Acad Sci. 1964 Dec 28;121:428–436. doi: 10.1111/j.1749-6632.1964.tb14214.x. [DOI] [PubMed] [Google Scholar]
- FELSENFELD G. The determination of cuprous ion in copper proteins. Arch Biochem Biophys. 1960 Apr;87:247–251. doi: 10.1016/0003-9861(60)90168-5. [DOI] [PubMed] [Google Scholar]
- Foldes A., Jeffrey P. L., Preston B. N., Austin L. Dopamine -hydroxylase of bovine adrenal medullae. A rapid purification procedure. Biochem J. 1972 Mar;126(5):1209–1217. doi: 10.1042/bj1261209. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Friedman S., Kaufman S. 3,4-dihydroxyphenylethylamine beta-hydroxylase. Physical properties, copper content, and role of copper in the catalytic acttivity. J Biol Chem. 1965 Dec;240(12):4763–4773. [PubMed] [Google Scholar]
- Friedman S., Kaufman S. An electron paramagnetic resonance study of 3,4-dihydroxyphenylethylamine beta-hydroxylase. J Biol Chem. 1966 May 25;241(10):2256–2259. [PubMed] [Google Scholar]
- Horwitz D., Alexander R. W., Lovenberg W., Keiser H. R. Human serum dopamine- -hydroxylase. Relationship to hypertension and sympathetic activity. Circ Res. 1973 May;32(5):594–599. doi: 10.1161/01.res.32.5.594. [DOI] [PubMed] [Google Scholar]
- Hörtnagl H., Winkler H., Lochs H. Membrane proteins of chromaffin granules, dopamine -hydroxylase, a major constituent. Biochem J. 1972 Aug;129(1):187–195. doi: 10.1042/bj1290187. [DOI] [PMC free article] [PubMed] [Google Scholar]
- LEVIN E. Y., LEVENBERG B., KAUFMAN S. The enzymatic conversion of 3,4-dihydroxyphenylethylamine to norepinephrine. J Biol Chem. 1960 Jul;235:2080–2086. [PubMed] [Google Scholar]
- Lee C. Y., Scocca J. R. A common structural unit in asparagine-oligosaccharides of several glycoproteins from different sources. J Biol Chem. 1972 Sep 25;247(18):5753–5758. [PubMed] [Google Scholar]
- Nagatsu T., Udenfriend S. Photometric assay of dopamine- -hydroxylase activity in human blood. Clin Chem. 1972 Sep;18(9):980–983. [PubMed] [Google Scholar]
- Rush R. A., Geffen L. B. Radioimmunoassay and clearance of circulating dopamine- -hydroxylase. Circ Res. 1972 Sep;31(3):444–452. doi: 10.1161/01.res.31.3.444. [DOI] [PubMed] [Google Scholar]
- Segrest J. P., Jackson R. L., Andrews E. P., Marchesi V. T. Human erythrocyte membrane glycoprotein: a re-evaluation of the molecular weight as determined by SDS polyacrylamide gel electrophoresis. Biochem Biophys Res Commun. 1971 Jul 16;44(2):390–395. doi: 10.1016/0006-291x(71)90612-7. [DOI] [PubMed] [Google Scholar]
- Spiro R. G. Glycoproteins. Annu Rev Biochem. 1970;39:599–638. doi: 10.1146/annurev.bi.39.070170.003123. [DOI] [PubMed] [Google Scholar]
- Viveros O. H., Arqueros L., Kirshner N. Mechanism of secretion from the adrenal medulla. V. Retention of storage vesicle membranes following release of adrenaline. Mol Pharmacol. 1969 Jul;5(4):342–349. [PubMed] [Google Scholar]
- Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]
- Winkler H., Hörtnagl H., Smith A. D. Membranes of the adrenal medulla. Behaviour of insoluble proteins of chromaffin granules on gel electrophoresis. Biochem J. 1970 Jun;118(2):303–310. doi: 10.1042/bj1180303. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Zacharius R. M., Zell T. E., Morrison J. H., Woodlock J. J. Glycoprotein staining following electrophoresis on acrylamide gels. Anal Biochem. 1969 Jul;30(1):148–152. doi: 10.1016/0003-2697(69)90383-2. [DOI] [PubMed] [Google Scholar]