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Detection of the e14 and e15 rabbit allotypic specificities by immunodiffusion in peg agar

1973; Elsevier BV; Volume: 10; Issue: 6 Linguagem: Inglês

10.1016/0019-2791(73)90149-3

1878-237X

William C. Eby, Byung S. Kim, Sheldon Dray, Glendowlyn O. Young‐Cooper, Rose G. Mage,

Toxin Mechanisms and Immunotoxins

We studied the effect of an IgG anti-IgM on the dissociation of cell bound IgM anti-hapten antibody, as measured with fluid phase hapten. Methotrexate (MTX) covalently bound to the red cells surface was used as hapten; rabbit anti-MTX IgM and rabbit anti-allotype IgG reactive with the IgM were used as antibodies. The amount of cell bound antibodies was measured with 125I-labelled protein A. In the absence of the anti-allotype antibody, most of the anti-hapten IgM was prevented from reassociation by fluid phase hapten. In the presence of the anti-allotype IgG most of the anti-hapten IgM was non-dissociable, with about a 1000-fold increase in the apparent binding constant. We found that (1) dissociability of the anti-hapten IgM depended on the density of the cell bound hapten, (2) decrease in dissociability was a function of the anti-allotype antibody concn and (3) even in the presence of excess anti-allotype antibody dissociability was an inverse function of anti-hapten IgM concn.