The malate dehydrogenase isoenzymes from the mitochondria of chicken hearts have been partially resolved into separate pools. Reversible denaturation, in concentrated guanidine hydrochloride, does not change the isoenzyme distribution in each pool. This result suggests that the electrophoretic differences among the isoenzymes are not solely conformational in origin.
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Schechter et al. (1968) studied this question.
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