Size-dependent allosteric effects of monovalent cations on rabbit liver fructose-1,6-bisphosphatase.
Open Access
- 1 July 1976
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 251 (14), 4315-4321
- https://doi.org/10.1016/s0021-9258(17)33298-2
Abstract
No abstract availableThis publication has 35 references indexed in Scilit:
- The activation of rabbit muscle, liver, and kidney fructose bisphosphatases by histidine and citrateArchives of Biochemistry and Biophysics, 1974
- Activation of rabbit muscle fructose diphosphatase by EDTA and the effect of divalent cationsArchives of Biochemistry and Biophysics, 1972
- Purification and properties of a rabbit kidney fructose diphosphatase with neutral pH optimumArchives of Biochemistry and Biophysics, 1972
- Rabbit liver fructose 1,6-diphosphatase. Properties of the native enzyme and their modification by subtilisinArchives of Biochemistry and Biophysics, 1972
- Rabbit liver and rabbit kidney fructose diphosphatases: Catalytic properties of enzymes activated by coenzyme A and acyl carrier proteinArchives of Biochemistry and Biophysics, 1970
- Univalent cation activation of fructose 1,6-diphosphataseArchives of Biochemistry and Biophysics, 1970
- Enzymes Activated by Monovalent CationsScience, 1970
- Thallium-205 nuclear magnetic resonance as a probe for studying metal ion binding to biological macromolecules. Estimate of the distance between the monovalent and divalent activators of pyruvate kinaseJournal of the American Chemical Society, 1970
- Role of Mineral Elements with Emphasis on the Univalent CationsAnnual Review of Plant Physiology, 1966
- Reversible inactivation and inhibition of liver fructose-1, 6-diphosphatase by adenosine nucleotidesBiochemical and Biophysical Research Communications, 1963