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. 1972 Aug;111(2):392–396. doi: 10.1128/jb.111.2.392-396.1972

Purification and Properties of Nicotinamide Adenine Dinucleotide-Dependent d- and l-Lactate Dehydrogenases in a Group N Streptococcus

L Mou 1, D P Mulvena 1, H A Jonas 1, G R Jago 1
PMCID: PMC251295  PMID: 4340863

Abstract

Streptococcus lactis strain 760, a group N streptococcus, was found to possess nicotinamide adenine dinucleotide-dependent dehydrogenase activities for both the l(+) and the d(−) isomers of lactic acid. The two enzymes were isolated and purified and were found to differ with respect to pH optima, activation by fructose-1,6-diphosphate, pH and heat stability, and the temperature at which each enzyme was formed in the organism during growth. The presence of a racemase for lactic acid was not detected by the methods used.

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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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