The chymotrypsin-catalysed activation of bovine liver glutamate dehydrogenase

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Abstract
Ox liver glutamate dehydrogenase is activated by bovine pancreatic .alpha.-chymotrypsin, but the extent of activation is dependent on the age of the dehydrogenase preparation. The degree of activation is constant and the pseudo-first-order rate constant of activation is directly proportional to the concentration of proteinase used. Commercial preparations of .alpha.-chymotrypsin differ in their ability to produce a secondary inactivation phase, due to low tryptic contamination. The superactive form of glutamate dehydrogenase has an increased sensitivity to tryptic inactivation as compared with the native enzyme. Analysis of the activation by sodium dodecyl sulfate/polyacylamide-gel electrophoresis revealed that the subunit MW of superactive glutamate dehydrogenase differs by less than 5% from that of the native subunit.