title: [Kinetic properties of membrane dopamine-beta-hydroxylase. ].
abstract: We studied membrane bound dopamine-beta-hydroxylase (DBH) from chromaffin granules, in order to determine whether a biological form of immobilization of the enzyme altered its kinetic properties. The results obtained suggested that DBH either in soluble or solubilized form showed a ping-pong mechanism whereas the membrane bound DBH did not. Affinity for the substrate and the pH stability were lower in soluble or solubilized form than in membrane bound DBH.
authors.affiliation: Departamento de Bioquímica, Facultad de Farmacia, Ciudad Universitaria, Madrid 3, Espagne.
authors.forename: M T
authors.initials: MT
authors.lastname: Miras Portugal
authors.forename: A
authors.initials: A
authors.lastname: Jorda
authors.forename: A
authors.initials: A
authors.lastname: Santos Ruiz
mesh_terms: D000818:Animals; D002837:Chromaffin Granules / Q000201:enzymology*; D004299:Dopamine beta-Hydroxylase / Q000378:metabolism*; D006801:Humans; D007425:Intracellular Membranes / Q000201:enzymology*; D007527:Isoenzymes / Q000378:metabolism; D007700:Kinetics; D008565:Membrane Proteins / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D007527:Isoenzymes; D008565:Membrane Proteins; D004299:Dopamine beta-Hydroxylase