Association of the anti-hen egg lysozyme antibody HyHEL-5 with avian species variant and mutant lysozymes

Kari A. Shick, K. Asish Xavier, Arvind Rajpal, Sandra J. Smith-Gill, Richard C. Willson

Research output: Contribution to journalArticle

19 Scopus citations

Abstract

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°C to 37°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 ace buried and not in direct contact with the antibody.

Original languageEnglish (US)
Pages (from-to)205-214
Number of pages10
JournalBiochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Volume1340
Issue number2
DOIs
StatePublished - Jul 18 1997

Keywords

  • Antibody
  • Calorimetry
  • Enthalpy
  • Lysozyme
  • Molecular recognition

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Structural Biology
  • Biophysics

Fingerprint Dive into the research topics of 'Association of the anti-hen egg lysozyme antibody HyHEL-5 with avian species variant and mutant lysozymes'. Together they form a unique fingerprint.

Cite this