The incorporation of J chain into reassembled human immunoglobulin M.
Human IgM (immunoglobulin M) was reduced with 24mm-mercaptoethylamine. This atreatment resulted in complete dissociation to IgMs subunits and free J chain. Intr-subunit interchain disulphide bonds remained intact. The mixture then was encouraged to reoxidize. The schlieren pattern of the reoxidized mixture showed the presence of a considerable quantity of IgM in addition to residual IgMs. The isolated reassembled IgM did not dissociate in 5m-guanidinium hydrochloride. It apparently contained the same amount of covalently attached J chain as did native IgM. The J chain was a part of the high-molecular-weight Fc fragment obtained from the reassembled IgM.
D001665:Binding Sites; D002850:Chromatography, Gel; D004220:Disulfides; D004591:Electrophoresis, Polyacrylamide Gel; D005021:Ethylamines; D006146:Guanidines; D006801:Humans; D005779:Immunodiffusion; D007122:Immunoelectrophoresis; D007141:Immunoglobulin Fc Fragments; D007144:Immunoglobulin J-Chains; D007075:Immunoglobulin M; D008970:Molecular Weight; D010084:Oxidation-Reduction; D011485:Protein Binding; D011487:Protein Conformation; D011489:Protein Denaturation; D013438:Sulfhydryl Compounds; D014461:Ultracentrifugation
D004220:Disulfides; D005021:Ethylamines; D006146:Guanidines; D007141:Immunoglobulin Fc Fragments; D007144:Immunoglobulin J-Chains; D007075:Immunoglobulin M; D013438:Sulfhydryl Compounds