The binding of inhibitors to alpha-chymotrypsin at alkaline pH.
1. The binding of the competitive inhibitor N-acetyl-d-tryptophan amide to alpha-chymotrypsin has now been studied at pH values up to 10.6, by the technique of equilibrium dialysis. 2. This binding depends on the ionization of a group on the free enzyme with apparent pK(a) 9.3 at 5 degrees . 3. This group is tentatively identified as that responsible for an enzyme conformation change at high pH values, on which the catalytic activity of the enzyme also depends.
D000577:Amides; D055598:Chemical Phenomena; D002621:Chemistry; D002918:Chymotrypsin; D003956:Dialysis; D004798:Enzymes; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D011485:Protein Binding; D011489:Protein Denaturation; D013816:Thermodynamics; D014316:Tritium; D014364:Tryptophan
D000577:Amides; D004798:Enzymes; D014316:Tritium; D014364:Tryptophan; D002918:Chymotrypsin