Abstract
ELECTROPHORETICALLY separated lactate dehydrogenase isoenzymes differ from each other in several respects, including immunochemical specificity1,2, substrate affinities3,4 ability to utilize coenzyme analogues5, sensitivity to inhibitors6,7, thermal stability8 and substrate specificity9. Among the inhibitors which have been reported to exert different effects on the anodic and cathodic isoenzymes are sulphite, which preferentially inhibits the former6, and urea, which at certain concentrations inhibits the latter without much affecting the activity of the former10,11.
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