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Protein A Reactivity of Two Distinct Groups of Human Monoclonal IgM
Author(s) -
LIND I.,
HARBOE M.,
FØLLING I.
Publication year - 1975
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.1365-3083.1975.tb03726.x
Subject(s) - monoclonal antibody , immunoglobulin m , monoclonal , staphylococcus aureus , reactivity (psychology) , hemagglutination , protein a , antibody , chemistry , microbiology and biotechnology , biology , immunology , virology , immunoglobulin g , medicine , bacteria , pathology , genetics , alternative medicine
Fifteen human monoclonal IgM proteins could be divided into two groups based on their ability to inhibit binding of a labelled human monoclonal IgM (IgM‐Se) to Staphylococcus aureus Cowan 1 (IgM‐Se assay); seven were positive and eight were negative. We found complete agreement between positive reaction in the IgM‐Se assay, the presence of protein A reactivity in gel diffusion experiments, and high litres in an indirect haemagglutination test that detects antibodies to protein A—IgG complexes. The protein A precipitation patterns of IgM and autologous IgG were not identical.