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Characterization of a Calcium‐Binding IgG Myeloma Protein
Author(s) -
LINDGÄRDE F.,
ZETTERVALL O.
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.tb01258.x
Subject(s) - immunoglobulin light chain , calcium , myeloma protein , chemistry , calcium binding protein , binding site , binding protein , antibody , multiple myeloma , mole , immunoglobulin g , microbiology and biotechnology , biochemistry , biology , immunology , organic chemistry , gene
A calcium‐binding IgG myeloma protein (A. L.) has previously been described It has now been characterized as an IgG1 lambda protein with two independent binding sites for calcium ions. The sites are localized in the Fab regions. Isolated heavy chains showed no unequivocal binding activity, whereas the light chains were active. The apparent intrinsic association constant for protein A.L., as found by equilibrium dialysis, was 10 4 l/mol.