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. 1972 Aug;111(2):392-6.
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, D P Mulvena, H A Jonas, G R Jago

Purification and properties of nicotinamide adenine dinucleotide-dependent D- and L- lactate dehydrogenases in a group N streptococcus

L Mou et al. J Bacteriol. 1972 Aug.

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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