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J. Biochem, 1974, Vol. 76, No. 6 1253-1258
© 1974 Japanese Biochemical Society

research-article

Degradation of Guinea Pig IgG1 amd IgG2 by Splenic Acid Protease

Takahisa SHINOMIYA and Jiro KOYAMA

Department of Hygienic Chemistry, Faculty of Pharmaceutical Science, Hokkaido University Sapporo 060

The two subclasses of guinea pig IgG (IgG1 and IgG2) were digested at pH 3.5 with acid protease extracted from homologous spleens. Both IgG1 and IgG2 were digested in a fashion similar to rabbit and human IgG, giving rise to F(ab')2–, Fab-, and Fc-like fragments, the Fc-like fragments being easily digested to small peptides. The F(ab')2– and Fab-like fragments thus isolated were proved to be very similar in size and immunochemical properties to F(ab')2 and Fab fragments produced by pepsin [EC 3.4.23.1 [EC] ] and papain [EC 3.4.22.2 [EC] ] digestions. However, they were more susceptible to the proteolytic activity of acid protease than those of rabbit IgG and were degraded completely to dialyzable peptides as the digestion proceeded.


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