The cross-reactivity of rat IgE and IgG with solubilized receptors of rat basophilic leukemia cells.
Normal rat IgG-Sepharose binds the same two receptors from solubilized rat basophilic leukemia (RBL) cells as are bound by rat IgE-Sepharose. These receptors have previously been designated R and H, and have apparent mol. wts of 45,000 and 55,000, respectively. Inhibition studies indicate that, although soluble deaggregated IgG is capable of interacting with both receptors, its affinity is higher for H than for R. Conversely, soluble IgE preferentially interacts with R, but its affinity for H is somewhat higher than that of rat IgG. Control studies show that IgG receptor interaction to be specific in that it is significantly stronger than that obtained with F(ab')2 fragments or a variety of proteins having pIs approximating that of IgG.
D000818:Animals; D001491:Basophils / Q000276:immunology; D002460:Cell Line; D002846:Chromatography, Affinity; D003429:Cross Reactions; D004591:Electrophoresis, Polyacrylamide Gel; D007073:Immunoglobulin E / Q000276:immunology*; D007074:Immunoglobulin G / Q000276:immunology*; D007938:Leukemia / Q000276:immunology* / Q000473:pathology; D051381:Rats; D011919:Rats, Inbred Strains; D011971:Receptors, Immunologic / Q000187:drug effects / Q000276:immunology*; D012995:Solubility
D007074:Immunoglobulin G; D011971:Receptors, Immunologic; D007073:Immunoglobulin E