Metabolism of DrugsXL. Enzymatic Oxidation of Methylhexabital 3. Purification and Properties of 3-Hydroxy-methyihexabital Dehydrogenase***

Publisher Website
Google Scholar
Abstract
3-hydroxy-methylhexabital (3-OH-MHB) dehydrogenase was purified about 55-fold from a crude soluble fraction of rabbit liver. During the course of the purification, 3-OH-MHB dehydrogenase was separated from alcohol dehydrogenase. Purified 3-OH-MHB dehydrogenase required nicotinamide adenine (NAD+) or NADP+ as hydrogen acceptor. Km value for 3-OH-MHB was 9.6 x 10-5 M with NAD+ and 1.9x10-5 M with NADP+ at pH 9.6. Optimal pH for 3-OH-MHB was 9.5 with NAD+ and 10.6 with NADP+. The maximal rate with NAD+ was about twice as much as that with NADP+. The purified 3-OH-MHB dehydrogenase was specific for 3-OH-MHB, 3-OH-EHB and cyclohexen-3-ol. But several alcohols, which were substrates of alcohol dehydrogenase, glucose and some hydroxy steroids were not dehydro-genated by this dehydrogenase. Moreover, the alcoholic derivative of alkyl side-chain of barbiturate, such as (ti -l)-OH-seconal, was not metabolized.

This publication has 2 references indexed in Scilit: