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 antibody 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 with HyHEL-5 is enthalpically driven in the temperature range 10 degrees C to 37 degrees C. The calorimetric results indicate that the salt-links 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 characteristic 'quail' mutations affect the energetics of antibody/antigen association, even though they are buried and not in direct contact with the antibody.
Shick
K A
KA
Department of Chemical Engineering, University of Houston, TX 77204-4792, USA.
Xavier
K A
KA
Rajpal
A
A
Smith-Gill
S J
SJ
Willson
R C
RC
D000818:Animals; D000906:Antibodies / Q000737:chemistry / Q000276:immunology*; D000936:Antigen-Antibody Complex / Q000737:chemistry; D051379:Mice; D009113:Muramidase / Q000235:genetics / Q000276:immunology*; D009154:Mutation; D011784:Quail / Q000235:genetics*; D013816:Thermodynamics
D000906:Antibodies; D000936:Antigen-Antibody Complex; D009113:Muramidase