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Localization of the Binding Site on IgG for Solubilized Placental Fcγ Receptor
Author(s) -
MATRE R.,
TÖNDER O.
Publication year - 1984
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.1365-3083.1984.tb00901.x
Subject(s) - agglutination (biology) , receptor , microbiology and biotechnology , binding site , rosette formation , fragment crystallizable region , monocyte , rosette (schizont appearance) , chemistry , fc receptor , antibody , biology , immunology , biochemistry
Placental FcγR (FcR) inhibited the rosette formation between monocytes and rabbit IgG‐sensitized erythrocytes (EA), whereas the rosette formation with granulocytes was not impaired. Staphylococcal protein A (SpA) inhibited the rosette formation with both cell types. Results obtained in absorption and agglutination experiments showed that SpA blocked the binding of FcR to IgG, and C1 did not. Furthermore, FcR did not interfere with the binding of SpA to IgG, whereas C1 affected this binding. FcR apparently bind to the Cγ3 region. Since FcR inhibited the binding of EA to monocytes, the monocyte FcR binding site is probably also located within the Cγ3 region.