[Structural and immunochemical studies on carp (Cyprinus carpio L.) immunoglobulins. IV. In vitro reassociation of carp immunoglobulin].
Mildly reduced high molecular immunoglobulin and antibody of carp with tetrameric structure, carbohydrate content of 6 to 7% and absence of J-chain can reassociate to native molecules. The disulphide bonds between subunits and polypeptide chains are sensitive and can be completly splitted by treatment with only 1 mM DTE. One half of the immunoglobulins retained their high molecular structure as expression of strong non-covalent bonds between subunits of the tetrameric molecule. The other half of immunoglobulins dissociate into HL-halfmolecules. We suppose that carps possess 2 "typs of immunoglobulins" which differ in the tendency to aggregate to high molecular immunoglobulins.
D000818:Animals; D002241:Carbohydrates / Q000032:analysis; D002347:Carps / Q000276:immunology*; D003530:Cyprinidae / Q000276:immunology*; D004226:Dithioerythritol; D007136:Immunoglobulins; D046911:Macromolecular Substances; D008970:Molecular Weight
D002241:Carbohydrates; D007136:Immunoglobulins; D046911:Macromolecular Substances; D004226:Dithioerythritol
Strukturelle und immunchemische Untersuchungen am Immunglobulin des Karpfens (Cyprinus carpio L.) IV. In vitro Reassoziation von Karpfen-Immunglobulin.