Determination of Equilibrium Dissociation Constants

Therapeutic Monoclonal Antibodies: From Bench to Clinic

Volumn , Issue , 2009, Pages 503-524

  Ernst, Robin E ^a   High, Katrina N ^a   Glass, Tom R ^b   Zhao, Qinjian ^a  

^a MERCK RESEARCH LABORATORIES   (United States)

^b Sapidyne Instruments Incorporated   (United States)

Author keywords

Antibody characterization; Determination of equilibrium dissociation constants; Kinetic based dissociation constant determination by SPR based technology

Indexed keywords

EID: 80155195574     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9780470485408.ch22     Document Type: Chapter

References (26)

1. Alfthan, K. 1998. Surfaceplasmonresonancebiosensors as a tool in antibody engineering. Biosensor Bioelectronics 13:653-663.
2. Azimzadeh, A., J.L. Pellequer, and H.V. Van Regenmortel. 1992. Operational aspects of antibody affinity constants measured by liquid-phase and solid phase assays. J. Mol. Recogn. 5:9-18.
3. Blake, R.C., N. Ohmura, S.J. Lackie, et al. 2005. In Trends in Monoclonal Antibody Research, ed. M.A. Simmons, 1-36. New York: Nova Biomedical Books.
4. Blake, R.C. II, A.R. Pavlov, and D.A. Blake. 1999. Automated kinetic exclusion assays to quantify protein binding interaction in homogeneous solution. Anal. Biochem. 272:123-134.
5. Canziani, G.A., S. Klakamp, and D.G. Myszka. 2004. Kinetic screening of antibodies from crude hybridoma samples using Biacore. Anal. Biochem. 325:301-307.
6. Darling, R.J., and P.-A. Brault. 2004. Kinetic exclusion assay technology: Characterization of molecular interactions. Assay Drug Development Tech. 2:647-657.
7. Darling, R.J., U. Kuchibhotla, W. Glaesner, et al. 2002. Glycosylation of erythropoietin affects binding kinetics: Role of electrostatic interactions. Biochemistry 41:14524-14531.
8. Drake, A.W., D.G. Myszka, and S.L. Klakamp. 2004. Characterizing high-affinity antigen/antibody complexes by kinetic-and equilibrium-based methods. Anal. Biochem. 328:35-43.
9. Friguet, B., A.F. Chaffotte, L.D. Ohaniance, and M.E. Goldberg. 1985. Measurements of the true affinity constant in solution of antigen-antibody complexes by enzyme-linked immunosorbent assay. J. Immunol. Methods 77:305-319.
10. Goldberg, M.E., and L.D. Ohaniance. 1993. Methods for measurement of antibody/antigen affinity based on ELISA and RIA. Curr. Opin. Immunol. 5:278-281.
11. Goodrich, J.A., and J.F. Kugel. 2007. Binding and Kinetics for Molecular Biologists: Affinity Constants. New York: Cold Spring Harbor Laboratory Press.
12. High, K., Y. Meng, M. Washabaugh, and Q. Zhao. 2005. Determination of picomolar equilibrium dissociation constants in solution by enzyme-linked immunosorbent assay with fluorescence detection. Anal. Biochem. 347:159-161.
13. Huber, W., and F. Mueller. 2006. Biomolecular interaction analysis in drug discovery using surface plasmon resonance technology. Curr. Pharm. Design 12:3999-4021.
14. Karlsson, R., and A. Falt. 1997. Experimental design for kinetic analysis of protein-protein interactions with surface plasmon resonance biosensors. J. Immunol. Methods 200:121-131.
15. Karlsson, R., H. Roos, and L. Fagerstam. 1994. Kinetic and concentration analysis using BIA technology. Methods Companion Methods Enzymol. 6:99-110.
16. Limbird, L.E. 1996. Cell Surface Receptors: A Short Course on Theory and Methods, 2nd edition. New York: Springer.
17. Luginbuhl, B., Z. Kanyo, R.M. Jones, et al. 2006. Directed evolution of an anti-prion protein scFv fragment to an affinity of 1 pM and its structural interpretation. J. Mol. Biol. 363:75-97.
18. Meng, Y., K. High, J. Antonello, M. Washabaugh, and Q. Zhao. 2005. Enhanced sensitivity and precision in an enzyme-linked immunosorbent assay with fluorogenic substrates compared with commonly used chromogenic substrates. Anal. Biochem. 345:227-236.
19. Rathanaswami, P., J. Babcock, and M. Gallo. 2008. High-affinity binding measurements of antibodies to cell-surface expressed antigens. Anal. Biochem. 373:52-60.
20. Rathanaswami, P., S. Roalstad, L. Roskos, et al. 2005. Demonstration of an in vivo generated sub-picomolar affinity fully human monoclonal antibody to interleukin-8. Biochem. Biophys. Res. Commun. 334:1004-1013.
21. Rich, R.L., and D.G. Myszka. 2007a. Higher-throughput, label-free, real-time molecular interaction anlaysis. Anal. Biochem. 361:1-6.
22. Rich, R.L., and D.G. Myszka. 2007b. Survey of the year 2006 commercial optical biosensor literature. J. Mol. Recognit. 20:300-366.
23. Stenberg, E., B. Persson, H. Roos, et al. 1991. Quantitative determination of surface concentration of protein with surface plasmon resonance using radiolabelled proteins. J. Colloid Interface Sci. 143:513-526.
24. Stevens, F. 1987. Modification of an ELISA-based procedure for affinity determination: Correction necessary for use with bivalent antibody. Mol. Immunol. 24:1055-1060.
25. Towne, V., M. Will, B. Oswald, and Q. Zhao. 2004. Complexities in horseradish peroxidase-catalyzed oxidation of dihydroxyphenoxazine derivatives: Appropriate ranges for pH values and hydrogen peroxide concentrations in quantitative analysis. Anal. Biochem. 334:290-296.
26. Xie, L., M. Jones, T.R. Glass, et al. 2005. Measurement of the functional affinity constant of a monoclonal antibody for cell surface receptors using kinetic exclusion fluorescence immunoassay. J. Immunol. Methods 304:1-14.