A non-dissociable rabbit IgG-protein a complex.
Glutaraldehyde treatment of rabbit IgG antibody complexed with protein A of Staphylococcus aureus (SpA) enabled the complex (IgG2-SpA1)2 to maintain its molecular weight unchanged and to become non-dissociable at low pH and in excess of IgG. The glutaraldehyde-treated (IgG2-SpA1)2 complex had the same half-life, complement-activating capacity and ability to interact with the Fc receptor as the non-treated complex. Moreover, the glutaraldehyde-treated complex had a stronger immunosuppressive effect on the synthesis of anti-sheep red blood cell antibody than either the non-complexed antibody or the IgG antibody complexed with SpA but untreated with glutaraldehyde.
D000818:Animals; D000915:Antibody Affinity / Q000187:drug effects; D001666:Binding Sites, Antibody / Q000187:drug effects; D003168:Complement Fixation Tests; D005976:Glutaral / Q000494:pharmacology; D006386:Hemagglutination Tests; D007074:Immunoglobulin G / Q000032:analysis / Q000502:physiology*; D007075:Immunoglobulin M / Q000096:biosynthesis; D007165:Immunosuppression Therapy; D046911:Macromolecular Substances; D011817:Rabbits; D012397:Rosette Formation; D013205:Staphylococcal Protein A / Q000032:analysis / Q000502:physiology*
D007074:Immunoglobulin G; D007075:Immunoglobulin M; D046911:Macromolecular Substances; D013205:Staphylococcal Protein A; D005976:Glutaral