The Contribution of the α and β Chains to the Kinetics of Oxygen Binding to and Dissociation from Hemoglobin
- 1 January 1973
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 70 (1), 1-4
- https://doi.org/10.1073/pnas.70.1.1
Abstract
A new type of experiment in which hemoglobin is exposed briefly to oxygen has shown that the half-time of dissociation of oxygen from some partly oxygenated intermediates is about 1 msec at 20 degrees and 10 msec at 2 degrees . The rapid dissociation occurs selectively from one type of chain, provisionally identified as the beta-chain. Chains that show the rapid rate of dissociation of oxygen also bind rapidly. It follows that the kinetic equivalent of the Adair equation and the Monod-Wyman-Changeux model are quite unsuited to represent the kinetics of the oxygen-hemoglobin reaction. The reaction of oxygen with hemoglobin closely resembles that of the alkyl isocyanides and differs radically from that of carbon monoxide.Keywords
This publication has 11 references indexed in Scilit:
- Carbon Monoxide Binding by Hemoglobin and Myoglobin under Photodissociating ConditionsProceedings of the National Academy of Sciences, 1972
- The reaction of n-butyl isocyanide with human hemoglobin. II. The ligand-binding properties of the and chains within deoxyhemoglobin.1972
- An allosteric model of hemoglobin: I, kineticsJournal of Molecular Biology, 1971
- The Dissociation of the First Oxygen Molecule from Some Mammalian OxyhemoglobinsJournal of Biological Chemistry, 1971
- The Reaction of Oxygen with Hemoglobin and the Kinetic Basis of the Effect of Salt on Binding of OxygenJournal of Biological Chemistry, 1970
- A practical automatic data acquisition system for stopped-flow spectrophotometryComputers and Biomedical Research, 1969
- Reciprocal binding of oxygen and diphosphoglycerate by human hemoglobin.Proceedings of the National Academy of Sciences, 1968
- Observations on the Kinetics of the Reaction of Hemoglobin with OxygenJournal of Biological Chemistry, 1967
- The kinetics of dissociation of the first oxygen molecule from fully saturated oxyhaemoglobin in sheep blood solutionsProceedings of the Royal Society of London. B. Biological Sciences, 1955
- The equilibrium between oxygen and sheep haemoglobin at very low percentage saturationsThe Journal of Physiology, 1951