Purification and Properties of Pyridine Nucleotide-Independent l-Lactate Dehydrogenase from Polyporus circinatus
AUTOR(ES)
Funayama, Shigehiro
RESUMO
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 × 10−4 M and the oxalate inhibition constant was 1.5 × 10−4 M. The nature of the prosthetic group is discussed.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=245708Documentos Relacionados
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