The accuracy of our lactate dehydrogenase (EC 1.1.1.27) isoenzyme procedure, based on electrophoresis in thin-layer agarose, has previously been assessed (Clin. Chem. 22: 1995, 1976). We now show that the method is similarly accurate and precise for the specific measurements of lactate dehydrogenase isoenzyme-1 and -2. We have also determined the lactate dehydrogenase isoenzyme pattern in perip...

Cell-free extracts of Chlorella pyrenoidosa contained two enzymes capable of oxidizing d-lactate; these were glycolate dehydrogenase and NAD(+)-dependent d-lactate dehydrogenase. The two enzymes could be distinguished by differential centrifugation, glycolate dehydrogenase being largely particulate and NAD(+)-d-lactate dehydrogenase being soluble. The reduction of pyruvate by NADH proceeded mor...

We investigated metabolic engineering of fermentation pathways in Escherichia coli for production of optically pure Dor L-lactate. Several pta mutant strains were examined, and a pta mutant of E. coli RR1 which was deficient in the phosphotransacetylase of the Pta-AckA pathway was found to metabolize glucose to D-lactate and to produce a small amount of succinate by-product under anaerobic cond...

objective: infectious microorganisms are major sources of illness and death worldwide, and the leading cause of death in neonates. effective vaccination of this age group is of particular importance. the lack of a response and greater susceptibility to tolerance are two major features that limit the effectiveness of vaccines in neonates. in this study we compare the cellular immune response gen...

A rapid purification of lactate dehydrogenase and glycolate oxidase from lettuce (Lactuca sativa) leaves is described. The kinetics of both enzymes are reported in relation to their possible roles in the production of oxalate. Lettuce lactate dehydrogenase behaves like mammalian dehydrogenase, catalyzing the dismutation of glyoxylate to glycolate and oxalate. A model is proposed in which glycol...