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Structural Studies of Three IgG K Proteins from a Patient with Multiple Myeloma
Author(s) -
DWORSKY E.,
SLETTEN K.,
HARBOE M.,
WETTELAND P.
Publication year - 1980
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.1365-3083.1980.tb00068.x
Subject(s) - immunoglobulin light chain , myeloma protein , homogeneous , multiple myeloma , immunoelectrophoresis , chemistry , chain (unit) , antibody , heavy chain , microbiology and biotechnology , biology , genetics , immunology , mathematics , combinatorics , physics , astronomy
Three distinct IgG proteins of similar concentration and the same light‐chain type were demonstrated in a myeloma serum. The bonds between the heavy and light chains were split, and the isolated γ‐ and κ‐chains were characterized by crossed immunoelectrophoresis, subgroup determination and N‐terminal amino acid sequence. The studies showed that the IgG heterogeneity was due to differences in the primary structure of the variable parts of the κ‐chains. Two of the κ‐chains belonged to subgroup VκI, and one chain, the most anodic one, belonged to VκIII. The γ‐chains were homogeneous and belonged to subgroup V H III.