BINDING OF AUTOREACTIVE MOUSE ANTI-TYPE-II COLLAGEN ANTIBODIES DERIVED FROM THE PRIMARY AND THE SECONDARY IMMUNE-RESPONSE INVESTIGATED WITHTHE BIOSENSOR TECHNIQUE

The reactivity of autoantibodies to type II collagen, secreted by B ce lls isolated from the primary and the secondary immune response to rat type II collagen in DBA/1 mice, was investigated using BIAcore 2000 i nstrumentation. Assays were performed on both collagen and antibody su rfaces. These assays demonstrated a 100-fold difference in affinity be tween primary and secondary immune response antibodies. The difference in affinity was almost entirely due to differences in the dissociatio n rate constant. Somatic mutations in secondary clones were in one cas e associated with a 3-4-fold difference in affinity and in another cas e appeared to be without any effect on the binding activity.