ASSOCIATION OF THE ANTI-HEN EGG LYSOZYME ANTIBODY HYHEL-5 WITH AVIAN SPECIES VARIANT AND MUTANT LYSOZYMES

The energetics of association of the murine anti-hen egg lysozyme anti body HyHEL-5 with bobwhite quail lysozyme, California quail lysozyme, and the Arg45 --> Lys mutant of hen egg lysozyme was characterized by isothermal titration calorimetry. The association of each lysozyme wit h HyHEL-5 is enthalpically driven in the temperature range 10 degrees C to 37 degrees C. The calorimetric results indicate that the salt-lin ks between Arg45 and Arg68 of hen egg lysozyme and GluH50 on the HyHEL -5 paratope are energetically important in HyHEL-5/HEL association. In contrast to previous studies, the results suggest that the three char acteristic 'quail' mutations affect the energetics of antibody/antigen association, even though they are buried and not in direct contact wi th the antibody. (C) 1997 Published by Elsevier Science B.V.