Abstract
The oxidation of dry denatured egg albumin and dry myosin by molecular oxygen indicates that the direct oxidation of dry proteins containing free sulphydryl groups is a general reaction. Cupric ion was the most effective catalyst for the oxidation of denatured egg albumin in solution. The rate of the oxidation was measured as a function of cupric ion concentration, pH, and temperature. Since the catalytic oxidations of denatured egg albumin, glutathione, and cysteine have very similar activation energies, the mechanism of copper-catalyzed sulphydryl oxidation may be the same for the three compounds. Under the conditions studied, only sulphydryl groups of denatured egg albumin were oxidized. The oxidation of these groups proceeded beyond the disulphide stage.
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