Quantitative potentialities in enzyme cytochemistry. Modified Michaelis-Menten rate law applicable when a substrate diffuses slowly into an enzyme site
- 1 March 1962
- journal article
- research article
- Published by Elsevier in Journal of Theoretical Biology
- Vol. 2 (2) , 117-128
- https://doi.org/10.1016/0022-5193(62)90040-1
Abstract
No abstract availableThis publication has 15 references indexed in Scilit:
- Rate behavior and concentration profiles in geometrically constrained enzyme systemsArchives of Biochemistry and Biophysics, 1957
- Diffusion and simultaneous chemical reactions: III. The degree of localization achieved in cytochemical staining proceduresBulletin of Mathematical Biology, 1956
- Approximate treatment of diffusion into a cylindrical enzyme system obeying Michaelis-Menten kineticsBiochimica et Biophysica Acta, 1956
- Diffusion and simultaneous chemical reactions: II. The equations of those systems in which transport occurs from one region to an adjoining regionBulletin of Mathematical Biology, 1955
- The inference of intracellular enzymatic properties from kinetic data obtained on living cells. II. A study of hexokinase and invertase as cellular components of Baker's yeastJournal of Cellular and Comparative Physiology, 1955
- The inference of intracellular enzymatic properties from kinetic data obtained on living cells. I. Some kinetic considerations regarding an enzyme enclosed by a diffusion barrierJournal of Cellular and Comparative Physiology, 1955
- Diffusion and simultaneous chemical reactions: I. A method for solving the equations of some systems in which a fixed concentration exists at a boundaryBulletin of Mathematical Biology, 1955
- The determination of enzyme inhibitor constantsBiochemical Journal, 1953
- Temperatures in Solids during Heating or CoolingIndustrial & Engineering Chemistry, 1942
- The Determination of Enzyme Dissociation ConstantsJournal of the American Chemical Society, 1934