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.
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Research Article| January 01 1974
The incorporation of J chain into reassembled human immunoglobulin M
Manuel J. Ricardo, Jr. ;
Biochem J (1974) 137 (1): 79–83.
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Manuel J. Ricardo, Franklin P. Inman; The incorporation of J chain into reassembled human immunoglobulin M. Biochem J 1 January 1974; 137 (1): 79–83. doi: https://doi.org/10.1042/bj1370079
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