A kinetic interpretation of the allosteric model of Monod, Wyman, and Changeux
- 1 October 1968
- journal article
- Published by Wiley in FEBS Letters
- Vol. 1 (5) , 346-348
- https://doi.org/10.1016/0014-5793(68)80150-4
Abstract
No abstract availableKeywords
This publication has 8 references indexed in Scilit:
- Alternative to allosterism and cooperativity in the interpretation of enzyme kinetic dataBiochemistry, 1968
- Treatment of Enzyme Kinetic DataPublished by Elsevier ,1967
- THE BINDING OF NICOTINAMIDE-ADENINE DINUCLEOTIDE TO YEAST D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE: TEMPERATURE-JUMP RELAXATION STUDIES ON THE MECHANISM OF AN ALLOSTERIC ENZYMEProceedings of the National Academy of Sciences, 1966
- The interpretation of non-hyperbolic rate curves for two-substrate enzymes. A possible mechanism for phosphofructokinaseBiochemical Journal, 1966
- 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
- Initial Steady State Velocities in the Evaluation of Enzyme-Coenzyme-Substrate Reaction Mechanisms.Acta Chemica Scandinavica, 1957
- A Note on the Kinetics of Enzyme ActionBiochemical Journal, 1925