gamma-Globulin from human blood serum was incubated in thermostat at 37 degrees within 15, 30, 45, 60 and 72 days. Amount of readily and poorly hydrolyzed amide groups as well as an increase in amino acid content were estimated in the protein at zero time and at these periods. The sterility of the preparation was examined in each case. Spontaneous deamidation of gamma-globulin, observed during incubation, caused an increase in negative charge and altered electrophoretic mobility of the protein molecule. gamma-Globulin was attacked by prothelin more effectively as amount of amide groups was decreased in the protein. Spontaneous deamidation appears to be one of reasons of the protein molecules ageing.
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