Temperature dependence of the effects of some monohydric alcohols on the oxygen affinity of hemoglobin: Determination and analysis of thermodynamic parameters
- 1 January 1981
- journal article
- research article
- Published by Wiley in Biopolymers
- Vol. 20 (1) , 53-63
- https://doi.org/10.1002/bip.1981.360200105
Abstract
No abstract availableThis publication has 17 references indexed in Scilit:
- Effect of some organic cosolvents on the reaction of hemoglobin with oxygenBiopolymers, 1981
- Thermodynamic aspects of the co-operativity in four-step oxygenation equilibria of haemoglobinJournal of Molecular Biology, 1979
- Effect of some monohydric alcohols on the functional stability of bovine liver ?-galactosidaseBiopolymers, 1979
- Effect of some monohydric alcohols on the oxygen affinity of hemoglobin: Relevance of solvent dielectric constant and hydrophobicityBiopolymers, 1979
- Haemoglobin: The structural changes related to ligand binding and its allosteric mechanismJournal of Molecular Biology, 1979
- Structure and function of haemoglobinProgress in Biophysics and Molecular Biology, 1976
- Hydrophobic interaction and structural changes in the solventBiopolymers, 1975
- Thermodynamical analysis of oxygen equilibrium of stripped hemoglobinBiochemical and Biophysical Research Communications, 1973
- On the nature of allosteric transitions: A plausible modelJournal of Molecular Biology, 1965
- DIELECTRIC CONSTANTS OF SOME ORGANIC SOLVENT-WATER MIXTURES AT VARIOUS TEMPERATURESJournal of the American Chemical Society, 1932