Molecular Heterogeneity and Evolution of Enzymes

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Abstract
The observations described indicate the molecular heterogeneity of the lactic dehydrogenases obtained from different tissues and from different animals. It is possible to classify animals by their enzymatic properties. Change in enzyme structure may have been of significance in the establishment of new species. Lactic dehydrogenases of the heart may have undergone considerably greater evolutionary changes than those of the skeletal muscles. The results outlined in this article may be of value in studying the interrelationship and origin of species. This may be of particular importance in connection with the flat fish, since the origin of this group of fish is at present quite unresolved. Investigations may eventually indicate whether certain peptide chains have been altered during species evolution, as well as in individual differentiation. It is evident from the data presented that the coenzyme analogues (some of which have been used previously and some of which have been recently synthesized) are valuable adjuncts in detecting the heterogeneity of dehydrogenases. Studies with crystalline dehydrogenase may elucidate the part of the enzyme molecule undergoing structural change during evolution.