A Study of the Native-Denatured (N_??_D) Transition in Lysozyme

III. Effect of Alteration of Net Charge by Acetylation

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Measurement of the enzymic activity and fluorescence properties showed that the gross con-formation of acetylated lysozyme [EC 3.2.1.17] is very similar to that of the native enzyme.
On the other hand, protease digestion, t-butyl hypochloride modification and thermal denaturation experiments performed on native, acetylated, and guanidinated lysozymes showed that acetylation caused a small but significant shift of the N_??_D transition to the right. Thus it can be concluded that charge balance in a protein plays an important role in maintaining its conformation.
The difference between equilibrium and kinetic methods of monitoring protein denatura-tion was also clarified.