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Protein A Reactivity of Various Mammalian Immunoglobulins
Author(s) -
GOUDSWAARD J.,
DONK J. A.,
NOORDZIJ A.,
DAM R. H.,
VAERMAN J.P.
Publication year - 1978
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.1365-3083.1978.tb00492.x
Subject(s) - polyclonal antibodies , size exclusion chromatography , antibody , affinity chromatography , ammonium sulfate precipitation , sepharose , protein g , monoclonal antibody , chemistry , immunoglobulin g , immunoglobulin m , protein a , ion chromatography , biochemistry , biology , chromatography , microbiology and biotechnology , immunology , enzyme
Serum samples and immunoglobulin fractions of eight mammalian species were applied to a Sepharose‐protein A column. As with the human immunoglobulin subclasses IgG1, IgG2 and IgG4, all examined animal IgG classes and subclasses were bound to a greater or lesser extent to protein A. However, the binding of IgG1 of ruminants was very poor. Polyclonal IgM and IgA of the pig, the dog and the cat may be separated in protein A reactive and protein A non‐reactive fractions. In addition, monoclonal canine IgM and IgA partially reacted with protein A. In combination with methods such as ammonium sulphate precipitation, ion exchange chromatography and gel‐filtration, affinity chromatography with protein A is recommended for the rapid purification of certain Ig (sub)classes of a number of mammalian species.