Key result
A rapid stopped-flow kinetic assay utilizing high pyruvate concentrations can accurately determine the total amount and ratio of heart and muscle lactate dehydrogenase isoenzymes in under a minute.
Stopped-flow kinetics provides a rapid method to quantify and differentiate LDH isoenzymes in tissue and serum samples.
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Enables rapid LDH isoenzyme analysis in animal models; leaves open human validation and clinical translation.
Stopped-flow kinetics indicate that human and chicken heart-type(4) lactate dehydrogenases (LDH) become inhibited as DPNH is oxidized in the presence of high concentrations of pyruvate. This inhibition is much less marked with the human and chicken muscle-type(4) enzymes. The initial rates and the difference in inhibition between the two types of enzyme have made it possible to determine the amount of, as well as the ratio between, the two types of LDH that are present in a given sample by a single kinetic assay. The stopped-flow kinetic method has been used to analyze amounts of LDH isoenzyme in different tissues, as well as in serum.
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Bishop et al. (1972) studied LDH isoenzyme analysis. Stopped-flow kinetic assay was evaluated on Ratio of H and M subunits of LDH. A rapid stopped-flow kinetic assay utilizing high pyruvate concentrations can accurately determine the total amount and ratio of heart and muscle lactate dehydrogenase isoenzymes in under a minute.
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