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Binding of Fragments of Human IgG to Solid‐phase C3b Measured by Enzyme‐linked Immunosorbent Assay (ELISA)
Author(s) -
HAUTANEN A.
Publication year - 1981
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.1365-3083.1981.tb00132.x
Subject(s) - polyclonal antibodies , chemistry , enzyme , immunoglobulin g , antibody , microbiology and biotechnology , fragment crystallizable region , biochemistry , receptor , biology , immunology
The binding of human IgG and different fragment of IgG to C3b adsorbed in polystyrene tubes has been studied by the enzyme‐linked immunosorbent Heat‐denatured polyclonal IgG and F(ab') 2 and Fab fragments of IgG bound to solid‐phase C3b Heat‐denatured Fc fragments of IgG also had some reactivity with C3b, but at significantly higher concentrations than F(ab') 2 and Fab fragments. The binding of heat‐denatured IgG could not be completely inhibited by the addition of heat‐denatured F(ab') 2 fragments in tenfold excess The results suggest that the binding of heat‐denatured IgG to solid‐phase C3b is mediated through the Fab and Fc portions binding of denatured IgG to solid‐phase C3b is mediated through the Fab and Fc portions of IgG molecules.