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Rabbit secretory immunoglobulin A (sIgA) was digested with papain in the absence of reducing agent and four fractions were isolated by gel filtration. Three of the four fractions, undigested sIgA, Fc~,, and Fabz, have previously been characterized (Hanly et ai. (1973), Biochemistry 12, 733); the fourth fraction (approximately 15% of the total protein) was identified as Fab,-like material by its sedimentation and antigenic properties. Each of the four fractions was analyzed for the allotypic specificities controlled by the f and g loci by quantitative precipitation of the radiolabeled fractions with anti-f or anti-g antisera. The f allotypic specificities

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Two allotypes of rabbit secretory IgA have been identified with antisera obtained by cross-immunization of rabbits with secretory IgA. The two antisera, anti-t61 and anti-t62, each reacted by double diffusion analysis with secretory IgA from some but not all rabbits. Both anti-t61 and anti-t62 reacted with purified free secretory component obtained from whey. Thus, anti-t61 and anti-t62 are identifying allotypic specificities on secretory component. Genetic studies revealed that t61 and t62 are controlled by allelic genes at an autosomal locus. The t locus is not closely linked to the VHa, Cαf and Cαg (heavy chain) loci nor to the b (light chain) locus of immunoglobulins.