Distinctions between the two-state and sequential models for cooperative ligand binding.
- 1 January 1977
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 74 (1) , 139-143
- https://doi.org/10.1073/pnas.74.1.139
Abstract
The 2-state and sequential models for positive cooperativity in ligand binding can produce significantly different theoretical binding curves when presented in a Scatchard plot. The conditions that produce the greatest differences were examined. The theoretical differences were used to select the 2-state model as the best model for describing the binding of acetylcholine to [Torpedo californica electroplax] acetylcholine receptors that were solubilized by Triton X-100 and sodium cholate.This publication has 10 references indexed in Scilit:
- The control of pyruvate kinase of Escherichia coli. Binding of substrate and allosteric effectors to the enzyme activated by fructose 1,6-bisphosphateBiochemistry, 1976
- Subunit interactions in yeast glyceraldehyde-3-phosphate dehydrogenaseBiochemistry, 1975
- Conversion of high affinity acetylcholine receptor from Torpedo californica electroplax to an altered formArchives of Biochemistry and Biophysics, 1975
- Cooperative Interactions of HemoglobinAnnual Review of Biochemistry, 1975
- Extensions of the allosteric model for hemoglobin. II. Consequences of functional nonequivalence of the α and β chainsBiochemistry, 1974
- Kinetics of Allosteric EnzymesAnnual Review of Biophysics and Bioengineering, 1974
- General method for the quantitative determination of saturation curves for multisubunit proteinsBiochemistry, 1970
- 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 Oxygen Equilibrium of Hemoglobin and Its Structural InterpretationProceedings of the National Academy of Sciences, 1935