Interaction of lysozyme with synthetic anti-lysozyme D1.3 antibody fragments studied by affinity chromatography and surface plasmon resonance.
Synthetic antibody fragments of monoclonal anti-lysozyme antibody D1.3 have been tested on binding with hen egg white lysozyme using immunoaffinity chromatography and surface plasmon resonance. Upon immunoaffinity chromatography, peptides containing one or two complementarity determining regions (CDRs) of D1.3 show interaction with lysozyme. Surface plasmon resonance with immobilized CDR peptides showed that this interaction is not based on the antigen-antibody interaction. Nevertheless, these peptides could be useful as ligands for the purification of lysozyme from a mixture of proteins.
Lasonder
E
E
Laboratory of Medical Microbiology, University of Groningen, Netherlands.
Bloemhoff
W
W
Welling
G W
GW
D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal / Q000378:metabolism*; D001666:Binding Sites, Antibody; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002645:Chickens; D002846:Chromatography, Affinity / Q000379:methods*; D005260:Female; D007128:Immunoglobulin Fragments / Q000378:metabolism*; D007158:Immunologic Techniques; D008969:Molecular Sequence Data; D009113:Muramidase / Q000276:immunology*
D000911:Antibodies, Monoclonal; D007128:Immunoglobulin Fragments; D009113:Muramidase