A Study of the Native-Denatured (N_??_D) Transition in Lysozynne
II. Kinetic Analysis of Protease Digestion
1976 Volume 80 Issue 6 Pages 1313-1318
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1976 Volume 80 Issue 6 Pages 1313-1318
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 (K0) of the N_??_D transition of the protein. Alteration of the net charge of lysozyme by acetylation caused a shift of the N=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_??_D transition is related to the susceptibility of lysozyme to protease digestion and it is estimated that the N_??_D transition in proteins is generally im-portant in the intracellular catabolism of proteins.
