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Purification and Properties of Pyridine Nucleotide-Independent L-Lactate Dehydrogenase from Polyporus circinatus

Instituto de Bioquímica da Universidade Federal do Paraná, e Divisão de Bioquímica do IBPT. Caixa Postal, 939, Curitiba, Paraná, Brazil

ABSTRACT

Cell extracts of Polyporus circinatus grown on lactate catalyze the reduction of 2,6-dichlorophenolindophenol by L-lactate without the participation of nicotinamide adenine dinucleotide or nicotinamide adenine dinucleotide phosphate. The enzyme has been purified 78-fold and was homogenous by disc gel electrophoresis. The optimal pH was found to be 6.7. The Michaelis constant for L-lactate was 5.9 x 10^–4 M and the oxalate inhibition constant was 1.5 x 10^–4 M. The nature of the prosthetic group is discussed.