Association of the anti-hen egg lysozyme antibody HyHEL-5 with avian species variant and mutant lysozymes.
Biochim Biophys Acta
; 1340(2): 205-14, 1997 Jul 18.
Article
en En
| MEDLINE
| ID: mdl-9252107
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.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Codorniz
/
Muramidasa
/
Anticuerpos
Tipo de estudio:
Risk_factors_studies
Límite:
Animals
Idioma:
En
Revista:
Biochim Biophys Acta
Año:
1997
Tipo del documento:
Article
País de afiliación:
Estados Unidos
Pais de publicación:
Países Bajos