The local distribution of glycyl-glycine dipeptidase (EC 3.4.13.1) from cat nervous tissue was studied. Using disc-electrophoresis, the multiplicity of the enzyme molecular forms was demonstrated. Glycyl-glycine dipeptidase from water extract and the partially purified enzyme forms revealed three similar or identical values of the pH optimum. The curves for the dependence of the reaction rate versus substrate concentrations for all the three enzyme forms under study are S-shaped. The kinetic data and the values of the Hill coefficient calculated by different methods are suggestive of allosteric properties of the cat brain enzyme.
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