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

Edwin Lasonder; Wim Bloemhoff; Gjalt W. Welling

doi:10.1016/0021-9673(94)00125-1

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

Edwin Lasonder^*, Wim Bloemhoff, Gjalt W. Welling

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

11 Citations (Scopus)

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.

Original language	English
Pages (from-to)	91-98
Number of pages	8
Journal	Journal of Chromatography A
Volume	676
Issue number	1
DOIs	https://doi.org/10.1016/0021-9673(94)00125-1
Publication status	Published - 29 Jul 1994
Externally published	Yes

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10.1016/0021-9673(94)00125-1

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

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.",

author = "Edwin Lasonder and Wim Bloemhoff and Welling, {Gjalt W.}",

note = "Funding information: We thank Dr J. Foote (Cambridge, UK) for his generous gift of monoclonal antibody hLys6 and Dr. M.H.J. Ruiters of the Biomedical Technology Centre, University of Groningen for the use of the BIAcore instrument. This research was supported by the Technology Foundation (STW) grant No. GGN99.1924.",

year = "1994",

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doi = "10.1016/0021-9673(94)00125-1",

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T1 - Interaction of lysozyme with synthetic anti-lysozyme D1.3 antibody fragments studied by affinity chromatography and surface plasmon resonance

AU - Lasonder, Edwin

AU - Bloemhoff, Wim

AU - Welling, Gjalt W.

N1 - Funding information: We thank Dr J. Foote (Cambridge, UK) for his generous gift of monoclonal antibody hLys6 and Dr. M.H.J. Ruiters of the Biomedical Technology Centre, University of Groningen for the use of the BIAcore instrument. This research was supported by the Technology Foundation (STW) grant No. GGN99.1924.

PY - 1994/7/29

Y1 - 1994/7/29

N2 - 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.

AB - 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.

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

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