The binding of three competitive inhibitors,
N-acetyl-D-tryptophan has been studied, N-acetyl-L-tryptophan and amide N-acetyl-D-tryptophan, chymotrypsin on the pH range of 2 · 20-9 · 65 by the dialysis technique at equilibrium. 2. Within the limits of the experimental method, the binding of uncharged amide inhibitor is independent of pH in the range studied. 3. The connection of each enantiomer acids depends on the ionization of a group on the free enzyme, apparent pKa7 · 3. 4. It is shown that the results of the ionization group in the active site of the enzyme a net negative charge at pH above 7 · Development 3. 5. enzymes responsible groups are tentatively identified, and the importance of binding constants in terms of enzymatic catalysis is discussed.
