Abstract
1. 1. Very few mitochondria, undetectable levels of succinate dehydrogenase and glutamate dehydrogenase and significant activities of glutamate pyruvate transaminase, glutamate oxaloacetate transaminase and malate dehydrogenase were observed in the deeper foot muscle tissue of Concholepas concholepas. 2. 2. Malate dehydrogenase activity was resolved into two molecular forms, which differ in K m values for oxaloacetate and malate, and sensitivity to inhibition by α-ketoglutarate. 3. 3. In addition to reoxidation of NADH generated from glycolysis, the function of malate dehydrogenase is discussed in connection with octopine synthesis and oxidation in the foot muscle of C. concholepas. 4. 4. The results of initial rate and product inhibition studies of both forms of malate dehydrogenase are consistent with an Ordered Bi Bi kinetic mechanism, with NADH adding first and NAD + leaving last. Oxaloacetate substrate inhibition is suggested to result from formation of an enzyme-NAD +-oxaloacetate dead end complex.
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