Lactate dehydrogenase isozymes in the trunk and cardiac muscles of an antarctic teleost fish,Notothenia neglecta Nybelin

The distribution and kinetics of lactate dehydrogenase (LDH) isozymes in the red and white trunk muscles, and cardiac muscle of an antarctic teleost fish (Notothenia neglecta Nybelin) have been studied. Pyruvate inhibition of LDH in all three muscle types is very low, being less than 50% even at a concentration of 60mM pyruvate. Activity versus pyruvate concentration profiles are not significantly different for LDH in all three muscle types. The Michaelis constant (Km) for pyruvate was not significantly different for all three LDH's. Raising the assay temperature caused an increase in Km of similar form in all three muscle types, while Km was lowest at the lowest assay temperature (-1°C). When samples were run on a polyacrylamide gel, the bands stained specifically for LDH activity appeared at identical positions as those of the H2M2 band of the standards.It would appear therefore that the LDH isozyme found in the red and white trunk muscle ofN. neglecta is identical to that in cardiac muscle. This fact is discussed in relation to the physiological ecology of antaretic fishes, and the metabolic constraints imposed by their habitat, including their apparent low capacity for utilising glycolytic fuels.