Interactions of pig Fabμ and Fabα fragments with protein a fromStaphylococcus aureus
- 1 May 1980
- journal article
- research article
- Published by Springer Nature in Folia Microbiologica
- Vol. 25 (3) , 254-258
- https://doi.org/10.1007/bf02877347
Abstract
Forty % of serum IgM and 47 % of dimeric colostral IgA were bound to protein A-Sepharose. Fab μ and Fabα fragments showed a reactivity similar to that of the whole immunoglobulins. Complete elutions of IgM and IgA from the protein A-Sepharose were obtained in lower concentrations of MgCl2 than the complete elution of IgG. However, IgM and IgA were completely eluted at higher concentrations of MgCl2 in the presence of IgG than in its absence.Keywords
This publication has 18 references indexed in Scilit:
- The Binding of Murine IgM to Staphylococcal A ProteinScandinavian Journal of Immunology, 1978
- Classes and subclasses of rat immunoglobulins: Interaction with the complement system and with staphylococcal protein AImmunochemistry, 1978
- Protein A Reactivity of Two Distinct Groups of Human Monoclonal IgMScandinavian Journal of Immunology, 1975
- The in vivo opsonizing activity of Fab μ and F(c)5 μ fragments of pig immunoglobulin M to Escherichia coli 0 55 in newborn, precolostral pigletsImmunochemistry, 1975
- 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
- Peptic digestion of pig IgMImmunochemistry, 1974
- J chain in pig immunoglobulinsImmunochemistry, 1973
- The Cross-linking of Proteins with Glutaraldehyde and its use for the preparation of immunoadsorbentsImmunochemistry, 1969
- Immunoglobulin M Antibodies with Ten Combining SitesScience, 1968