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Title 

Binding kinetics of monoclonal antibody using antigen-β-galactosidase hybrid protein: application to measurement of peptide antigenicity

Authors 

Eun Wie ChoMyung Kyu LeeKil Lyong KimKyung Soo Hahm

Publisher 

Taylor & Francis

Issue Date 

1995

Citation 

Journal of Immunoassay and Immunochemistry, vol. 16, no. 4, pp. 349-363

Keywords 

antigen-β-galactosidase hybrid proteinBinding kineticscompetitive ELISAmonoclonal antibodypeptidebeta galactosidasehybrid proteinprotein asynthetic peptide

Abstract 

A simple method for determination of binding kinetics of a solid-phase antibody using antigen-β-galactosidase hybrid protein was evaluated. To minimize conformational change of the antigen binding site of the antibody when directly binding to a microtiter plate, the microtiter plate was precoated with protein A. The binding and free antigen concentrations were directly obtained from the β-galactosidase activity. This method can be used for analyses of the equilibrium dissociation constant (K(D)), and the association (K(ass)) and dissociation (Kd(iss)) rate constants. Peptide antigenicity was also analyzed by competitive ELISA using this method. Since both antigen-β-galactosidase and the peptide used are localized in the fluid-phase, the proper affinity constant (K(A)) of the peptide can be estimated from the K(D) value of the antigen-β-galactosidase-antibody interaction, and from the IC50 value of the peptide.

ISSN 

0197-1522

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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