Dopamine-β-Hydroxylase: A Tetrameric Glycoprotein
- 1 August 1973
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 70 (8), 2253-2255
- https://doi.org/10.1073/pnas.70.8.2253
Abstract
Dopamine-beta-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-beta-hydroxylase is a tetrameric glycoprotein.Keywords
This publication has 19 references indexed in Scilit:
- A common structural unit in asparagine-oligosaccharides of several glycoproteins from different sources.1972
- Photometric Assay of Dopamine-β-Hydroxylase Activity in Human BloodClinical Chemistry, 1972
- Radioimmunoassay and Clearance of Circulating Dopamine-β-HydroxylaseCirculation Research, 1972
- Dopamine β-hydroxylase of bovine adrenal medullae. A rapid purification procedureBiochemical Journal, 1972
- Human erythrocyte membrane glycoprotein: A re-evaluation of the molecular weight as determined by SDS polyacrylamide gel electrophoresisBiochemical and Biophysical Research Communications, 1971
- Membranes of the adrenal medulla. Behaviour of insoluble proteins of chromaffin granules on gel electrophoresisBiochemical Journal, 1970
- GlycoproteinsAnnual Review of Biochemistry, 1970
- Tissue fractionation and catecholamines—III: Intracellular distribution of endogenous inhibitors of dopamine-β-hydroxylase in adrenal medullaBiochemical Pharmacology, 1970
- The Reliability of Molecular Weight Determinations by Dodecyl Sulfate-Polyacrylamide Gel ElectrophoresisJournal of Biological Chemistry, 1969
- Mechanism of secretion from the adrenal medulla. V. Retention of storage vesicle membranes following release of adrenaline.1969