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Lactate dehydrogenase isozymes in the eye and heart and skeletal muscles of some decapods


, : Lactate dehydrogenase isozymes in the eye and heart and skeletal muscles of some decapods. Zhurnal Evolyutsionnoi Biokhimii i Fiziologii 12(6): 521-526

Properties of lactate dehydrogenase (LDH) in the eye, heart and muscles of Hemigrapsus sanguineus, Paralithodes camtschatica, Erimacrus isenbeckii, Pandalus latirastrus and Pagurus brachiomastus were studied with acrylamide gel electrophoresis and kinetics analysis. LDH in all the tissues of all the representatives studied was specific for L-pyruvate and lactate; it migrated in electrophoresis as a single band revealing low mobility towards anode. The isoenzyme from P. camtschatica and P. latirastrus differed from the isoenzymes of other animals studied by higher mobility towards anode that reflected higher negative value of its total charge. The LDH isoenzymes in all animals studied resembled the A4 (LDH5) of the vertebrates being unstable to the denaturing action of high temperature and being unaffected by high concentrations of pyruvate up to 1.0 .cntdot. 10-3 M. In contrast to the A4 of mammals, this LDH displayed enhancement of the reaction rate and decrease of the Km values on increase in the NAD+ and NADH concentrations, in the presence of high or low lactate and pyruvate concentrations. The isoenzymes displayed catalytic activity in the presence of NADP, the Km values for pyruvate in the presence of equimolar (2.25 mM) concentrations of NADH or NADPH were practically identical and were within the limits of 14-26 .cntdot. 10-5 M. MW of the LDH assessed by gel filtration was 130,000-140,000. The decapod LDH isoenzyme is homologous in certain properties to the homotetrameric A4 form of the vertebrates.

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