Interaction of heavy and light chains of myeloma immunoglobulin with pooled normal chains: quantitative analysis of association and restoration of idiotype.
We have analyzed in vitro recombinants between the isolated heavy (H) or light (L) chains of mouse myeloma protein MOPC-21 and L or H chains of normal mouse serum immunoglobulin (Ig). In the first series of experiments using fixed H chain and solubilized L chain, we have found out that only about 30% of normal L chain pool interact efficiently with individual H chain. Moreover, fractions with different affinity to H-MOPC-21 appeared to exist among normal L chains. In the second set of experiments recombination of H and L chains in solution was used. Examination of recombinants between myeloma H chain and normal L chains revealed a set representing 6% of L chain repertoire capable of forming MOPC-21-like idiotypic structure.
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D000915:Antibody Affinity; D000916:Antibody Diversity; D007143:Immunoglobulin Heavy Chains; D007130:Immunoglobulin Idiotypes; D007147:Immunoglobulin Light Chains; D066298:In Vitro Techniques; D051379:Mice; D009194:Myeloma Proteins / Q000276:immunology / Q000378:metabolism*
D000911:Antibodies, Monoclonal; D007143:Immunoglobulin Heavy Chains; D007130:Immunoglobulin Idiotypes; D007147:Immunoglobulin Light Chains; D009194:Myeloma Proteins