Abstract
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.
Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
