RT Journal Article SR Electronic(1) A1 Dhariwal, K. R. A1 Venkitasubramanian, T. A.YR 1978 T1 Purification and Properties of β-Hydroxybutyrate Dehydrogenase from Mycobacterium phleiatcc354 JF Microbiology, VO 104 IS 1 SP 123 OP 126 DO https://doi.org/10.1099/00221287-104-1-123 PB Microbiology Society, SN 1465-2080, AB β-Hydroxybutyrate dehydrogenase (EC 1.1.1.30) was purified 145-fold from Mycobacterium phlei 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. K m 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, Ca2+ and partially by Mn2+. The enzyme did not require metal ions and was insensitive to EDTA, glutathione, dithiothreitol, β-mercaptoethanol and cysteine., UL https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-104-1-123