Abstract
Rabbit IgG antibodies against bacterial α-amylase were treated with trypsin in a medium free of any added reducing agent. The 5S fragments were isolated from the tryptic digest by fractionation with ammonium sulfate followed by gel filtration through Sephadex G-100 and were subsequently characterized in various ways. The tryptic 5S fragments could (1) form specific precipitate with corresponding antigen, (2) neutralize amylase actity, (3) react with anti-Fab but not with anto-Fc sera, (4) failed to induce passive cutaneous anaphylaxis in guinea pig. The 5S fragments (5) were separated into two populations by chromatography on carboxymethyl-cellulose, (6) differed in electrophoretic mobility from the original IgG, and (7) upon treatment with cysteine were split into 3·5S univalent fragments. The tryptic 5S fragments closely resembled the peptic 5S fragments with respect to antigenic structure and sedimentation characteristics.
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