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Lactate dehydrogenase ec 1.1.1.27 in human skeletal muscle


, : Lactate dehydrogenase ec 1.1.1.27 in human skeletal muscle. Acta Physiologica Scandinavica Supplementum (436): 1-32

Human skeletal muscle was studied. There was a correlation between the total lactate dehydrogenase [LDH (E.C. 1.1.1.27)] activity and fiber type distribution. The LDH activity decreased with increasing percent slow twitch (ST) or type I fibers; this decrease was related to an elevated relative activity of the heart specific LDH (H-LDH) isozymes in the ST fibers. The LDH isozyme pattern was influenced by environmental factors such as training. The relative activity of H-LDH increased after endurance training, although extreme anaerobic training did not induce any measurable changes either in total LDH activity or in LDH isozyme pattern. Strong product inhibition of total LDH activity was present even at physiologically low product concentrations in an optimal in vitro system indicating a regulatory function of LDH in glycogenolysis in vivo during physical activity. The intracellular distribution of the LDH isozymes in human skeletal muscle agrees with earlier findings in animal tissues. LDH of predominant muscle specific type was bound to the sarcoplasmic reticulum and the outer mitochondrial membrane, while H-LDH was found in the mitochondria.

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