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Measuring Bioactivity: KI, IC50 and EC50

  • Eric MarÉchalEmail author
Chapter

Abstract

Which quantity permits a characterisation of the performance of a bioactive molecule? How can a test be created so as to detect the effect of a molecule on a given target? Are there any general rules to respect? The design of a test is a complex problem dealt with in chapter 3; here we emphasise that, above all, the target must be a limiting factor in the reaction system.

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References

  1. BADET B. (2002) La catalyse enzymatique. Numéro spécial de L’Actualité Chimique 256: 5-30, EDP SciencesGoogle Scholar
  2. CHENG H.C. (2002) The power issue: determination of KB or Ki from IC50. A closer look at the Cheng-Prusoff equation, the Schild plot and related power equations. J. Pharmacol. Toxical. Methods 46: 61-71CrossRefGoogle Scholar
  3. CHENG H.C. (2004) The influence of cooperativity on the determination of dissociation constants: examination of the Cheng-Prusoff equation, the Scatchard analysis, the Schild analysis and related power equations. Pharmacol. Res. 50: 21-40CrossRefGoogle Scholar
  4. CHENG Y.C., PRUSOFF W.H. (1973) Relationship between the inhibition constant (Ki) and the concentration of inhibitor which causes 50 percent inhibition (IC50) of an enzymatic reaction. Biochem. Pharmacol. 22: 3099-3108CrossRefGoogle Scholar
  5. CORNISH-BOWDEN A. (2004) Fundamentals of Enzyme Kinetics (3rd edition). Portland Press, 438 p.Google Scholar
  6. LINEWEAVER H., BURK D. (1934) The determination of enzyme dissociation constants. J. Am. Chem. Soc. 56: 658-666.CrossRefGoogle Scholar
  7. MICHAELIS M., MENTEN M.L. (1913) Die Kinetic der Invertinworkung. Biochem. Z. 49: 333-369Google Scholar
  8. PELMONT J. (2005) Enzymes. Catalyseurs du monde vivant. Collection Grenoble Sciences. PUG, 1039 p.Google Scholar
  9. SCHUCK P. (1997) Use of surface plasmon resonance to probe the equilibrium and dynamic aspects of interactions between biological macromolecules. Annu. Rev. Biophys. Biomol. Struct. 26: 541-566CrossRefGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 2011

Authors and Affiliations

  1. 1.Laboratory of Plant Cell Physiology, Institute of Life Sciences Research and Technologies CEACNRS - CEA - INRA - Joseph Fourier UniversityGrenobleFrance

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