A study of the native-denatured (N in equilibrium with D) transition in lysozyme. II. Kinetic analysis of protease digestion.
Kinetic analyses of the protease digestion of several chemical derivatives of lysozyme [EC 3.2.1.17] showed that only the D(denatured) state of the protein is digested and that the reaction velocity is proportional to the equilibrium constant (KD) of the N in equilibrium with D transition of the protein. Alteration of the net charge of lysozyme by acetylation caused a shift of the N in equilibrium with D transition to the right (ten-fold increase in KD compared to that of native enzyme). Both the formation of a lysozyme-inhibitor complex and the introduction of a covalent bond in the lysozyme molecule restricted the transition. The magnitude of the N in equilibrium with D transition is related to the susceptibility of lysozyme to protease digestion and it is estimated that the N in equilibrium with D transition in proteins is generally important in the intracellular catabolism of proteins.
D000107:Acetylation; D002918:Chymotrypsin; D007700:Kinetics; D009113:Muramidase; D010447:Peptide Hydrolases; D011402:Pronase; D011487:Protein Conformation; D011489:Protein Denaturation; D013381:Subtilisins
D009113:Muramidase; D010447:Peptide Hydrolases; D013381:Subtilisins; D002918:Chymotrypsin; D011402:Pronase