The kinetics of rat liver and heart mitochondrial β-hydroxybutyrate dehydrogenase

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Abstract
The kinetic mechanisms of the .beta.-hydroxybutyrate dehydrogenase [EC 1.1.1.30] from rat heart and liver mitochondria were investigated. Both enzymes show an Ordered Bi Bi mechanism and there are no major differences in the kinetic constants. In both cases, the solubilized enzyme, re-activated with phosphatidylcholine, shows kinetic properties very similar to those of the enzyme bound to the mitochondrial membrane.