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- Title
Comparison of Mechanisms of Interaction between Protein A from Staphylococcus aureus and Human Monoclonal IgG, IgA and IgM in Relation to the Classical Fcγ and the Alternative F(ab')<sub>2</sub>ε Protein A Interactions.
- Authors
Inganäs, M.
- Abstract
Four purified human monoclonal IgG, IgA and IgM proteins were tested for their inhibitory effect on the binding of protein-A-reactive 125I-IgE and 125I-Fcγ, respectively, to protein-A- Sepharose. Only IgG mycloma proteins significantly inhibited the binding of 125I-Fcγ to protein- A-Sepharose, whereas most, but not all, myeloma proteins, irrespective of their immunoglobulin class and with varying efficiency, inhibited the binding of protein-A-reactive 125I-IgE to protein- A-Sepharose. The inhibitory effect of IgG and IgA proteins on the binding of protein-A-reactive 125I-IgE was retained in the respective F(ab′)2 fragments, whereas the inhibitory effect of IgG proteins on the binding of 125I-Fcγ to protein-A-Sepharose was exclusively expressed in the Fcγ fragment. In addition to the classical Fcγ-protein A interaction, the results indicate the existence of a common and variably expressed protein A reactivity in at least four of five human immunoglobulins. The data suggest that an interaction with protein A cannot be used as a criterion for subclass differentiation of IgA and IgM.
- Subjects
MONOCLONAL antibodies; IMMUNOGLOBULINS; PROTEINS; STAPHYLOCOCCUS aureus; IMMUNOCHEMISTRY; IMMUNOLOGY
- Publication
Scandinavian Journal of Immunology, 1981, Vol 13, Issue 4, p343
- ISSN
0300-9475
- Publication type
Article
- DOI
10.1111/j.1365-3083.1981.tb00143.x