An Analysis on the Slope of Scatchard Plots
Open Access
- 1 December 1976
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 71 (2), 529-532
- https://doi.org/10.1111/j.1432-1033.1976.tb11141.x
Abstract
The Scatchard plot, [X]b/[E]t[X] versus [X]b/[E]t where [X]b denotes the concentration of bound ligand, [E]t the total concentration of the binding protein and [X] the free ligand concentration, was designed originally for plotting data of ligand binding to a macromolecule possessing identical non‐interacting ligand binding sites. However, the plot is used for describing cooperative binding processes. In such cases, the slope of the Scatchard plot is not then equal to minus the intrinsic association constant any more. The meaning of the slope in such cases is a complex function of the binding parameters and its exact interpretation depends on the particular model used to analyze the binding data. In this communication, the meaning of the slope of the Scatchard plot is analyzed in terms of the different allosteric models.This publication has 7 references indexed in Scilit:
- The Role of Negative Cooperativity and Half-of-the-Sites Reactivity in Enzyme RegulationCurrent Topics in Cellular Regulation, 1976
- The quantitative interpretation of maximum in Scatchard plotsFEBS Letters, 1974
- NEGATIVE COOPERATIVITY IN REGULATORY ENZYMESProceedings of the National Academy of Sciences, 1969
- Comparison of Experimental Binding Data and Theoretical Models in Proteins Containing Subunits*Biochemistry, 1966
- On the nature of allosteric transitions: A plausible modelJournal of Molecular Biology, 1965
- THE ATTRACTIONS OF PROTEINS FOR SMALL MOLECULES AND IONSAnnals of the New York Academy of Sciences, 1949
- THE HEMOGLOBIN SYSTEMJournal of Biological Chemistry, 1925