Purification and Properties of Leucine Dehydrogenase of Bacillus natto KMD 1126

概要

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Leucine dehydrogenase of Bacillus natto KMD 1126 was purified by ammonium sulfate fractionation, diethylaminoethyl cellulose chromatography, Sephadex G 200 gel filtration, and preparative electrophoresis. The homogeneity of purified enzyme was demonstrated by disc gel electrophoresis. Optimum pH for oxidative deamination was 10.7,whereas it was 9.5 for reductive amination. The molecular weight of the enzyme was 360000 daltons as determined by gel filtration on Sephadex G 200. Nicotinamide adenine dinucleotide (NAD^+) in the oxidative deamination and reduced NAD in the reductive amination assay could not be replaced by nicotinamide adenine dinucleotide phosphate (NADP^+) or reduced NADP. L-Leucine, L-isoleucine, L-valine, and L-alanine were accepted as substrates but not the following amino acids : L-glutamic acid, L-aspartic acid, L-glutamine, L-asparagine, L-serine, L-threonine, L-cysteine, L-lysine, and D-amino acids. p-Chloromercuribenzoate (PCMB) inactivated the enzyme and it was reversed by cysteine. This enzyme had not antitumor activity on Ehrlich ascites carcinoma bearing mice.
社団法人日本薬学会の論文
1977-04-25