title: [Interaction between immobilized antibodies and the antigen-enzyme complex].
abstract: The interaction between immobilized antibodies against human immunoglobulin G (IgG) and the immunoenzyme complex IgG-peroxidase (IgG-P) was studied. The complex was obtained by covalent binding of IgG to peroxidase modified by sodium periodate. Study of the IgG-P binding kinetics and dissociation of the antibody-(IgG-P) complex showed that the antibodies immobilized on Sepharose reversibly interacted with IgG-P, similar to the antigen-antibody reaction in solution. The efficient values of the binding constants for the antibodies binding to Sepharose covalently and through the antigen-antibody bond are (2,2+/-0,5) 10(8) M-1 and (4,2+/-0,2) 10(8) M-1, respectively. The nature of a carrier and the immobilization method used do not significantly affect the rate of the complex binding to the antibodies. The activation energy of the reaction of IgG-P binding to the antibodies immobilized on Sepharose covalently and through the antigen-antibody bond is 7,3 and 4,1 kcal/mole, respectively. A procedure of titration of immobilized antibodies active sites with the antigen-enzyme complex is discussed.
mesh_terms: D000936:Antigen-Antibody Complex; D000937:Antigen-Antibody Reactions; D000941:Antigens; D002151:Calorimetry; D006801:Humans; D007074:Immunoglobulin G; D010544:Peroxidases; D011485:Protein Binding; D012685:Sepharose
chemical_list: D000936:Antigen-Antibody Complex; D000941:Antigens; D007074:Immunoglobulin G; D012685:Sepharose; D010544:Peroxidases
vernacular_title: Izuchenie v3aimodeĭstviia immobilizovannykh antitel s kompleksom antigen-perment.