Affinity chromatography of bacterial lactate dehydrogenases.

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