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. 1978 Jun 1;171(3):543–547. doi: 10.1042/bj1710543

Affinity chromatography of bacterial lactate dehydrogenases.

N Kelly, M Delaney, P O'Carra
PMCID: PMC1183998  PMID: 666726

Abstract

The affinity system used was the immobilized oxamate derivative previously used to purify mammalian lactate dehydrogenases. The bacterial dehydrogenases specific for the L-stereoisomer of lactate behaved in the same way as the mammalian enzymes, binding strongly in the presence of NADH. The D-lactate-specific enzymes, however, did not show any biospecific affinity for this gel. The L-specific enzymes could be purified to homogeneity in one affinity-chromatographic step. The D-specific enzymes could be efficiently separated from the L-specific ones and could then be further purified on an immobilized NAD derivative. The mechanism of activation of the lactate dehydrogenase from Streptococcus faecalis by fructose 1,6-bisphosphate was investigated by using the immobilized oxamate gel.

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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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