Effect of the modification and denaturation of glutamate dehydrogenase on its polarographic behaviour

The peak occurring in the differential pulse polarogram of native bovine glutamate dehydrogenase (GDH) at about −1.5 V in neutral media is influenced by the modification of some amino acid residues of the enzyme. The reactions of GDH with acetic anhydride and diethylpyrocarbonate (which modify lysine and histidine residues, respectively, and decrease essentially the basicity of their nitrogens) result in a shift of the peak potential to more …