[Immunochemical study of the conformational properties of the variable and constant domains of the light chain of mouse MOPC myeloma immunoglobulin].
The antigenic activity of variable (V) and constant (C) domains of mouse myeloma MOPC 21 light (L) chain has been used as a probe of their conformational state. The conformational properties of L-monomers, L-dimers and native IgG1 MOPC 21 protein were investigated by the reaction of inhibition of radioimmunoadsorbtion. Antibodies against the C-domain and different regions of V-domain were used in these experiments. It was shown that V-domain of L-monomers has sharp local conformational disruptions as compared with the native protein, while the conformational state of C-domain remains stable in monomers, dimers and native protein. It was found that the coinformational flexibility of different parts of V-domain of L-monomers is not equal. The antigenic activity of V-domain is partly restored in L-dimers, reaching the conformational state close to that of v-domain in the native protein. The possible interrelation between the conformational properties of V-domains and their functional activity is discussed.
D000818:Animals; D001666:Binding Sites, Antibody; D000939:Epitopes; D007127:Immunoglobulin Constant Regions / Q000276:immunology; D007147:Immunoglobulin Light Chains / Q000276:immunology; D007135:Immunoglobulin Variable Region / Q000276:immunology; D007136:Immunoglobulins; D051379:Mice; D009194:Myeloma Proteins / Q000276:immunology; D009374:Neoplasms, Experimental; D010954:Plasmacytoma / Q000032:analysis; D011487:Protein Conformation; D011864:Radioimmunosorbent Test
D000939:Epitopes; D007127:Immunoglobulin Constant Regions; D007147:Immunoglobulin Light Chains; D007135:Immunoglobulin Variable Region; D007136:Immunoglobulins; D009194:Myeloma Proteins
Immunokhimicheskoe issledovanie konformatsionnykh svoĭstv variabel'nogo i postoiannogo domenov legkoĭ tsepi mielomongo immunoglobulina myshi MOPC 21.