Abstract
Summary
Rabbit gamma globulin antibody fractions, prepared by ammonium sulfate fractionation of pooled sera of rabbits immunized with formalin-killed Salmonella typhosa, were digested with pepsin. Extent of digestion was estimated by tyrosine present in dialyzable digest fragments. Digest fractions, which precipitated between 40%-60% ammonium sulfate saturation, had agglutinin titers equal to, or perhaps greater than, titers of undigested globulin. The major component of the 40%-60% fraction also migrated more slowly in the ultracentrifuge. This suggests that it has been possible to digest rabbit antibody globulin so that smaller molecules are obtained in a digest fraction which still maintains its agglutinin antibody activity.
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