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. 1974 Sep;119(3):1000–1005. doi: 10.1128/jb.119.3.1000-1005.1974

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

Shigehiro Funayama 1, Glaci T Zancan 1
PMCID: PMC245708  PMID: 4153027

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 × 10−4 M and the oxalate inhibition constant was 1.5 × 10−4 M. The nature of the prosthetic group is discussed.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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