Monoclonal antibodies to human insulin and their antigen binding behaviour.
Mouse monoclonal antibodies were raised against human insulin by somatic cell hybridization using the mouse myeloma line P3-X63-Ag8. Five cell lines were grown as ascites producing tumors. Insulin binding data were determined from six monoclonal antibodies by Scatchard analysis. Each anti-insulin hybridoma antibody gave a straight-line Scatchard plot confirming the homogeneity of their binding sites and their monoclonality. The equilibrium dissociation constants ranged from 2.20 X 10(-8) to 4.48 X 10(-10) mol/l. We could demonstrate positive as well as negative cooperativity of monoclonal insulin antibodies by performing insulin binding studies with defined mixtures of two different anti-insulin hybridoma antibodies.
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology*; D000915:Antibody Affinity; D000941:Antigens / Q000276:immunology; D006801:Humans; D006825:Hybridomas / Q000276:immunology; D007328:Insulin / Q000276:immunology* / Q000378:metabolism; D007700:Kinetics; D051379:Mice
D000911:Antibodies, Monoclonal; D000941:Antigens; D007328:Insulin