Hemoglobin Kinetics and the Effect of Organic Phosphates
- 6 December 1974
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 186 (4167), 929-932
- https://doi.org/10.1126/science.186.4167.929
Abstract
A kinetic model based on allosteric mechanisms of cooperativity fits the experimentally observed phosphate dependence of hemoglobin reactions. Subunit inequivalence is found to be important in analyzing hemoglobin kinetics. The observed increase in the rate of deoxygenation in the presence of organic phosphates is primarily related to the increased rate of dissociation of the second oxygen molecule.Keywords
This publication has 21 references indexed in Scilit:
- A general approach to co-operativity and its application to the oxygen equilibrium of hemoglobin and its effectorsJournal of Molecular Biology, 1974
- A new approach to the direct determination of the forth velocity constant l′4 in human hemoglobinBiochemical and Biophysical Research Communications, 1973
- Chain non-equivalence in nitric oxide binding to hemoglobinBiochemical and Biophysical Research Communications, 1973
- 31P-NMR studies of the release of diphospholygeric acid on carbon monoxide binding to hemoglobinBiochemical and Biophysical Research Communications, 1972
- A general model of cooperativity and its application to DPG inhibition of hemoglobin oxygenationBiochemical and Biophysical Research Communications, 1972
- Oxygen recombination kinetics following laser photolysis of oxyhemoblobinBiochemical and Biophysical Research Communications, 1972
- An allosteric model of hemoglobin: I, kineticsJournal of Molecular Biology, 1971
- Time dependent model for hemoglobin and allosteric enzymes. II.Biopolymers, 1971
- Organic phosphates and ligand binding in hemoglobinBiochemical and Biophysical Research Communications, 1970
- The effects of 2,3-diphosphoglycerate on the kinetics of deoxygenation of human hemoglobinBiochemical and Biophysical Research Communications, 1970