Different protein A immunosorbents may have different binding specificity for rat immunoglobulins.
Purified polyclonal immunoglobulin preparations representing the 4 rat IgG subclasses were tested for binding to Staphylococcus aureus protein A attached to 3 different solid phases (Staphylococcus aureus Cowan I bacteria, Sepharose CL4B and Sepharose 6MB). Protein A Sepharose CL4B showed higher reactivity with IgG1 and IgG2b than the staphylococci, whereas protein A Sepharose 6MB showed a lower uptake of these subclasses. No differences were seen for IgG2a and IgG2c. Protein A on different solid phases cannot be used interchangeably without confirmation of binding specificity.
D000818:Animals; D002846:Chromatography, Affinity / Q000379:methods; D007074:Immunoglobulin G / Q000276:immunology*; D007163:Immunosorbent Techniques; D051381:Rats / Q000276:immunology*; D013045:Species Specificity; D013205:Staphylococcal Protein A / Q000276:immunology*; D013211:Staphylococcus aureus / Q000276:immunology
D007074:Immunoglobulin G; D013205:Staphylococcal Protein A