Kinetics of co-operative ligand binding in proteins: The effects of organic phosphates on hemoglobin oxygenation
- 1 May 1976
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 103 (1), 89-126
- https://doi.org/10.1016/0022-2836(76)90054-1
Abstract
No abstract availableKeywords
This publication has 44 references indexed in Scilit:
- Analysis of the allosteric basis for positive and negative co-operativity and half-of-the-sites reactivity in yeast and rabbit muscle glyceraldehyde 3-phosphate dehydrogenaseJournal of Molecular Biology, 1975
- A general approach to co-operativity and its application to the oxygen equilibrium of hemoglobin and its effectorsJournal of Molecular Biology, 1974
- A mathematical model for structure-function relations in hemoglobinJournal of Molecular Biology, 1972
- 31P-NMR studies of the release of diphospholygeric acid on carbon monoxide binding to hemoglobinBiochemical 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
- 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
- On the nature of allosteric transitions: A plausible modelJournal of Molecular Biology, 1965
- Ueber einen in biologischer Beziehung wichtigen Einfluss, den die Kohlensäurespannung des Blutes auf dessen Sauerstoffbindung übt1Skandinavisches Archiv Für Physiologie, 1904