The Interactive Binding of Two Ligands by an Allosteric Protein
- 1 August 1977
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 78 (1) , 127-132
- https://doi.org/10.1111/j.1432-1033.1977.tb11721.x
Abstract
The equilibrium constants describing the simultaneous binding of the ligands AMP and 1-anilinonapthalene-8-sulfonate (ansyl) by phosphorylase b [rabbit muscle] were evaluated. The binding of a single molecule of AMP per dimer unit causes only a moderate reduction in the binding constant for a single molecule of ansyl, but reduces that for a 2nd molecule of ansyl by 10-fold. The binding of 2 molecules of AMP per dimer unit almost abolishes the binding of a single molecule of ansyl.This publication has 13 references indexed in Scilit:
- The use of nanosecond fluorometry in detecting conformational transitions of an allosteric enzymeBiopolymers, 1975
- Properties of the highly reactive mercapto groups of phosphorylase bBiochemistry, 1975
- Studies on the Interaction of Ligands with Phosphorylase b Using a Spin‐Label ProbeEuropean Journal of Biochemistry, 1972
- The analysis of the binding of two ligands by an allosteric proteinJournal of Theoretical Biology, 1972
- Influence of substrate and effectors on the binding of 1-anilino-8-naphthalenesulfonate by glycogen phosphorylaseBiochemistry, 1972
- The regulation of enzyme activity and allosteric transitionProgress in Biophysics and Molecular Biology, 1970
- Remarks on the kinetics of enzymes with interacting effector molecules. Tests of a configurational hypothesis in a quasi-equilibrium modelBiochemistry, 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
- [49a] Muscle phosphorylase bPublished by Elsevier ,1962