Similar to IgG from other animal species, chicken IgG hydrolyzed with papain and reducing agent is split into products with a sedimentation coefficient of 3.4 S. Approximately 30 to 50% of the products are dialyzable peptides. The average molecular weight of the subunits calculated from two independent determinations was 49,500 and 54,000.

The amino acid composition of the nondialyzable and dialyzable fractions of the digests were similar except that the values for valine and histidine were lower, and the value for threonine was higher in the nondialyzable fractions.

Immunoelectrophoresis of digested antibovine serum albumin (BSA) IgG revealed two antigenically distinct fragments. The electrophoretically-slow (S) fragment retained the ability to bind antigen specifically and the electrophoretically-fast (F) fragment was inactive in this respect.

An amorphous precipitate and a small amount of crystalline material formed on dialysis of digests against water or low ionic strength acid buffers. The precipitate contained part of the F fraction. No S fraction was detected in the precipitate.

Digests fractionated by carboxymethyl cellulose (CMC) chromatography using an acetate buffer gradient (pH 5.4) were eluted as two fractions, both containing the S and F fragments. At pH 6.0 only the S fraction was eluted from CMC in the second peak. A better separation of the S and F components was made by chromatography on diethylaminoethyl(DEAE)-cellulose and by starch block electrophoresis. Most preparations were eluted from DEAE-cellulose in three distinct peaks: namely, two active S components (S' and S") and an inactive F fragment.

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