β-Hydroxybutyrate dehydrogenase (EC was purified 145-fold from ATCC354 by ammonium sulphate fractionation and DEAE-cellulose chromatography. The pH optima for oxidation and reduction reactions were 8.4 and 6.8 respectively. The purified enzyme was specific for NAD, NADH, acetoacetate and D(-)-β-hydroxybutyrate. values for DL-β-hydroxybutyrate and NAD were 7.4 mM and 0.66 mM respectively. The enzyme was inactivated by mercurial thiol inhibitors and by heat, but could be protected by NADH, Ca and partially by Mn. The enzyme did not require metal ions and was insensitive to EDTA, glutathione, dithiothreitol, β-mercaptoethanol and cysteine.


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