The Binding of Murine IgM to Staphylococcal A Protein
- 1 May 1978
- journal article
- research article
- Published by Wiley in Scandinavian Journal of Immunology
- Vol. 7 (5) , 367-370
- https://doi.org/10.1111/j.1365-3083.1978.tb00466.x
Abstract
The binding of staphylococcal A protein [Staph A] to murine immunoglobulins [Ig] was previously thought to be restricted to the IgG2 and IgG3 classes. In this study, 5 IgM proteins were assessed for binding, and of these, 1 showed marked Staph A binding. Pepsin digestion of this IgM molecule produced several different sized fragments, and the binding studies with these fragments indicated that the binding site is in the CH2 [H chain constant region 2] domain.This publication has 6 references indexed in Scilit:
- Allotypes of mouse IgM immunoglobulinNature, 1977
- Binding of IgA to Protein‐A‐Containing Staphylococci: Relationship to SubclassesScandinavian Journal of Immunology, 1976
- Protein A Reactivity of Two Distinct Groups of Human Monoclonal IgMScandinavian Journal of Immunology, 1975
- Recognition of Two Distinct Groups of Human IgM and IgA Based on Different Binding to StaphylococciScandinavian Journal of Immunology, 1974
- Tryptic Fragments of Fc from Normal Human IgG and their Interaction with Staphylococcal Protein AScandinavian Journal of Immunology, 1974
- Definition of staphylococcal protein A reactivity for human immunoglobulin G fragmentsImmunochemistry, 1970