[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.