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A Monoclonal IgG Protein with Antibody‐Like Activity for Transferrin and with X Chains of an Unusual Molecular Size
Author(s) -
WERNET P.,
KICKHÖFEN B.,
WESTERHAUSEN M.,
SVEHAG S. E.
Publication year - 1974
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1974.tb01324.x
Subject(s) - transferrin , monoclonal antibody , size exclusion chromatography , chemistry , hemosiderosis , antibody , hemochromatosis , microbiology and biotechnology , biochemistry , molecular mass , cirrhosis , biology , medicine , immunology , enzyme
The serum of a patient with high serum iron and transferrin levels contained an abnormal brownish protein with a sedimentation coefficient of 9.9S. At pH 3.5 this protein dissociated, and on gel filtration it proved to be a complex of one molecule of monoclonal IgGI and two molecules of transferrin. At pH 7.6 the isolated 59 Fe‐labeled transferrin recombined with most of the separated IgGI, forming again the original complex. Of particular interest was that the polypeptide kappa chains of this IgG seemed to have a molecular size of 27,000 to 28,000 daltons. We came to the conclusion that the serum of this patient contained a monoclonal protein with antibody‐like specificity for normal transferrin. Transferin only circulated as a complex with this protein at high levels in the serum and probably accumulated in the liver, giving use to severe hemosiderosis and cirrhosis.