INTERACTION OF LYSOZYME WITH SYNTHETIC ANTILYSOZYME D1.3 ANTIBODY FRAGMENTS STUDIED BY AFFINITY-CHROMATOGRAPHY AND SURFACE-PLASMON RESONANCE

Citation
E. Lasonder et al., INTERACTION OF LYSOZYME WITH SYNTHETIC ANTILYSOZYME D1.3 ANTIBODY FRAGMENTS STUDIED BY AFFINITY-CHROMATOGRAPHY AND SURFACE-PLASMON RESONANCE, Journal of chromatography, 676(1), 1994, pp. 91-98
Citations number
25
Categorie Soggetti
Chemistry Analytical
Journal title
Volume
676
Issue
1
Year of publication
1994
Pages
91 - 98
Database
ISI
SICI code
Abstract
Synthetic antibody fragments of monoclonal anti-lysozyme antibody D1.3 have been tested on binding with hen egg white lysozyme using immunoa ffinity chromatography and surface plasmon resonance. Upon immunoaffin ity chromatography, peptides containing one or two complementarity det ermining regions (CDRs) of D1.3 show interaction with lysozyme. Surfac e plasmon resonance with immobilized CDR peptides showed that this int eraction is not based on the antigen-antibody interaction. Nevertheles s, these peptides could be useful as ligands for the purification of l ysozyme from a mixture of proteins.