Abstract
Earlier studies, which provided indirect evidence for the involvement of the Cγ2 domain of human immunoglobulin G (IgG) in human immunoglobulin G (IgG) in human monocyte binding, have been extended to further localise the site of interaction on human IgG. A number of IgGs from several different species and fragments of human IgGs were assayed for ability to inhibit the interaction of radio-labelled human IgG and the human monocyte. By comparison of the amino-acid sequences of those IgGs found to exhibit relatively tight, intermediate or weak binding to human monocyte Fc receptors we are able to postulate a possible monocyte-binding site on human IgG. In addition, the results have implications for the applicability of monoclonal antibodies and antisera when used in the presence of human monocytes and possibly macrophages.
| Original language | English |
|---|---|
| Pages (from-to) | 319-330 |
| Number of pages | 12 |
| Journal | Molecular Immunology |
| Volume | 23 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - Mar 1986 |
Keywords
- Amino Acid Sequence
- Animals
- Antibody Affinity
- Binding Sites, Antibody
- Cattle
- Complement Activating Enzymes/immunology
- Complement C1q
- Goats
- Guinea Pigs
- Hot Temperature
- Humans
- Immunoglobulin G/immunology
- Mice
- Monocytes/immunology
- Rats
- Receptors, Fc/immunology
- Sheep
- Swine
ASJC Scopus subject areas
- Immunology
- Molecular Biology