[Kinetic properties of membrane dopamine-beta-hydroxylase. ].
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.
Miras Portugal
M T
MT
Departamento de Bioquímica, Facultad de Farmacia, Ciudad Universitaria, Madrid 3, Espagne.
Jorda
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Santos Ruiz
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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
D007527:Isoenzymes; D008565:Membrane Proteins; D004299:Dopamine beta-Hydroxylase