The effect of temperature on the binding kinetics and equilibrium constants of monoclonal antibodies to cell surface antigens

Abstract

The effect of temperature on the kinetic association and dissociation binding parameters, and equilibrium constants of four monoclonal antibodies to the murine Ly-2.1 and Ly-3.1 antigens has been studied using flow cytometry. All four monoclonal antibodies were conjugated to FITC and their association to, and dissociation from, the surface of murine thymoma cells was observed at 15 sec intervals, at temperatures between 1 and 37°C. The initial association rate constant and the dissociation rate constant for each antibody at each temperature were calculated from graphs of the first-order reactions and it was demonstrated that an increase in temperature caused an increase in both association r..