Anaerobic glycolysis occurs when the concentration of oxygen is not sufficient for aerobic respiration. During anaerobic glycolysis, lactate dehydrogenase (LDH) converts pyruvate to lactate while oxidizing nicotinamide adenine dinucleotide (NADH). LDH exists as several isozymes in the body and is often used as a diagnostic test for tissue injury as a result. It is particularly useful to diagnose injury of heart, liver, kidney, muscle, brain, and lung tissue. This study involves the isolation of LDH from beef, mouse, and rat heart followed by its purification using various types of chromatography, including ion-exchange and affinity chromatography. A full kinetic study was performed on the purified LDH and was compared to a known LDH standard. Inhibition of LDH was studied through the synthesis and characterization of known inhibitors, such as oxamate. Kinetic studies of LDH are useful as it plays a major role in medical diagnostic tests.

Lactate dehydrogenase: A study of kinetics and inhibition

249th National Meeting (2015)

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