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Although most proteins are liable to denature in alkaline solution, ovalbumin is not only resistant to alkali but also converts to a stable form, s-ovalbumin. This interesting phenomenon has been extcnsively investigated by many workers,th6) However, thc mechanism for the stabilizatien is still unexplained, although small changes in conforrnation,2i shape3'4] and surface chargeS) have been reported・during the conversion of ovalbumin to s-ovalbumin. Ofthese many reports, there are no reports on the differences in covalent structure bctwecn thcsc protcins, Wc found that the deamidation of asparagine or glutamine in ovalbumin occurred during the conversion to s-ovalbumin. This finding may be important for elucidating the mechanism of the fbrmation of s-ovalbumin. This paper describes the deamidation of ovalbumin during the conversion to s-ovalbumin. Ovalbumin was prepared from fresh egg white by a crystallization method in sodium sulfate and recrystallized five times.T] s-Ovalbumin was prepared by the method of Smith and Back.3) A 5% ovalbumin solution in water was adjusted to pH 9.9 and kept at 55`C. The amide residues in ovatbumins werc measured by the arnounts of residual ammonia in ovalbumin hydrolyzates. After hydrolysis of ovalbumin in 3N HCI at 110UC for 3hr to deamidate it

Deamidation of ovalbumin during S-ovalbumin conversion.