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Isolation of IgG3 from Polyclonal Human IgG by Affinity Chromatography with Ricinus Agglutinin
Author(s) -
SALTVEDT E.,
NATVIG J. B.
Publication year - 1977
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.1365-3083.1977.tb02138.x
Subject(s) - polyclonal antibodies , affinity chromatography , chemistry , agglutinin , microbiology and biotechnology , monoclonal antibody , sepharose , biochemistry , glycoprotein , chromatography , lectin , antibody , biology , enzyme , immunology
Ricinus agglutinin purified to homogeneity reacts with serum glycoproteins containing terminal nonreducing galactose residues, including about 10% polyclonal IgG. To study the IgG subclass distribution of this reaction, four monoclonal IgG1 proteins, two IgG2, four IgG3, and two IgG4 proteins were tested by affinity chromatography experiments with insolubilized ricinus agglutinin. Only the IgG3 proteins reacted, and the reactive sites were localized to the Fc fragment. Passage of polyclonal human IgG through a ricinus agglutinin–Sepharose column, followed by elution with lactose, permitted the isolation of IgG3 from normal polyclonal IgG.