Abstract
Isatin inhibits rat testicular alkaline phosphatase (E.C. 3.1.3.1) uncompetitively. The hyperbolic curve relating inhibition as a function of substrate concentration; the persistence of inhibition after the tertiary structure of the enzyme was altered by heat denaturation, exposure to urea or papain digestion; the small changes in entropy, free energy and enthalpy in the presence of isatin, and the number of isatin molecules (n = 1.29) combining with 1 molecule of enzyme indicate the non-allosteric nature of inhibition.

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