Abstract
1. 1. The supernatant and mitochondrial forms of muscle malate dehydrogenase (E.C. 1.1.1.37) isolated from two closely related species of shrimp have molecular weights and hydrodynamic properties similar to those previously reported for the corresponding enzymes of vertebrates. 2. 2. The catalytic properties of these species more closely resemble those of the vertebrate malate dehydrogenases than those of lower eukaryotes. 3. 3. The electrophoretic behavior of the shrimp malate dehydrogenases indicates that they are comprised of two subunits. 4. 4. The subunits of the shrimp enzymes are non-identical and give rise to three electrophoretically distinguishable isoenzymes of each dehydrogenase.
Published Version
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