A simple model for a regulatory enzyme
- 30 September 1977
- journal article
- research article
- Published by Elsevier in Journal of Theoretical Biology
- Vol. 68 (3) , 391-413
- https://doi.org/10.1016/0022-5193(77)90068-6
Abstract
No abstract availableThis publication has 20 references indexed in Scilit:
- The mechanistic interpretation of initial velocity and product inhibition data arising from enzyme catalysed reactions whose catalytic cycle is unbranchedJournal of Theoretical Biology, 1975
- Kinetic manifestations of allosteric interactions in models of regulatory enzymes with “indirect” co-operativityJournal of Theoretical Biology, 1974
- Intestinal alkaline phosphatase. Catalytic properties and half of the sites reactivityBiochemistry, 1974
- Allosteric kinetics of pyruvate kinase of Saccharomyces carlsbergensisJournal of Molecular Biology, 1973
- A mathematical model for structure-function relations in hemoglobinJournal of Molecular Biology, 1972
- The regulation of enzyme activity and allosteric transitionProgress in Biophysics and Molecular Biology, 1970
- Binding of cytidine triphosphate to aspartate transcarbamylaseBiochemical and Biophysical Research Communications, 1970
- On the all0steric interaction between 5'AMP and orthophosphate on phosphorylase b. Quantitative kinetic predictionsBiochemical and Biophysical Research Communications, 1967
- On the nature of allosteric transitions: A plausible modelJournal of Molecular Biology, 1965
- Typical behaviour of some simple models of enzyme actionTransactions of the Faraday Society, 1958