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Interaction of lysozyme with synthetic anti-lysozyme D1.3 antibody fragments studied by affinity chromatography and surface plasmon resonance.

作者信息

Lasonder E, Bloemhoff W, Welling G W

机构信息

Laboratory of Medical Microbiology, University of Groningen, Netherlands.

出版信息

J Chromatogr A. 1994 Jul 29;676(1):91-8. doi: 10.1016/0021-9673(94)00125-1.

Abstract

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.

摘要

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