Antibody-antigen interactions measured by surface plasmon resonance: global fitting of numerical integration algorithms

The interactions between adenylate kinase (AK) and a monoclonal antibody against AK (McAb3D3) were examined by means of optical biosensor technology, and the sensograms were fitted to four models using numerical integration algorithms. The interaction of a solution of McAb3D3 with immobilized AK fol...

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Bibliographic Details
Published in:Journal of biochemistry (Tokyo) Vol. 130; no. 4; p. 553
Main Authors: Luo, J, Zhou, J, Zou, W, Shen, P
Format: Journal Article
Language:English
Published: England 01.10.2001
Subjects:
Adenylate Kinase - immunology
Algorithms
Animals
Antibodies, Monoclonal - immunology
Antibody Affinity
Binding Sites, Antibody
Binding, Competitive
Enzyme-Linked Immunosorbent Assay - methods
Hydrogen-Ion Concentration
Kinetics
Rabbits
Surface Plasmon Resonance - methods
ISSN:0021-924X
Online Access:Get more information
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Summary:The interactions between adenylate kinase (AK) and a monoclonal antibody against AK (McAb3D3) were examined by means of optical biosensor technology, and the sensograms were fitted to four models using numerical integration algorithms. The interaction of a solution of McAb3D3 with immobilized AK follows a double exponential function and the data fitted well to an inhomogeneous ligand model. The interaction of a solution AK with immobilized McAb3D3 follows a single exponential function and the data fitted well to a pseudo-first order reaction model. The true association constants of AK binding to McAb3D3 in solution were obtained from competition BIAcore measurements. The difference in results obtained with solid-phase BIAcore and competition BIAcore may be due to rebinding of the dissociated analyte to the immobilized surface. The results obtained with BIAcore are compared to those obtained by ELISA methods. We suggest that the best method for analysis of BIAcore data is direct, global fitting of sensorgrams to numerical integration algorithms corresponding to the different possible models for binding.
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ISSN:0021-924X
DOI:10.1093/oxfordjournals.jbchem.a003018