PH dependence of the Adair constants of human hemoglobin. Nonuniform contribution of successive oxygen bindings to the alkaline Bohr effect.
Open Access
- 1 March 1975
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 250 (6) , 2227-2231
- https://doi.org/10.1016/s0021-9258(19)41706-7
Abstract
No abstract availableKeywords
This publication has 18 references indexed in Scilit:
- pH dependence of the shape of the hemoglobin-oxygen equilibrium curveBiochimica et Biophysica Acta (BBA) - Protein Structure, 1973
- Analyses of oxygen equilibriums of native and chemically modified human adult hemoglobins on the basis of Adir's stepwise oxygenation theory and the allosteric model of Monod, Wyman, and ChangeuxBiochemistry, 1973
- Stereochemistry of Cooperative Effects in Haemoglobin: Haem–Haem Interaction and the Problem of AllosteryNature, 1970
- Inhibition of Bohr Effect after Removal of C-Terminal Histidines from Haemoglobin β-ChainsNature, 1970
- Studies on the function of abnormal hemoglobins I. An improved method for automatic measurement of the oxygen equilibrium curve of hemoglobinBiochimica et Biophysica Acta (BBA) - Protein Structure, 1970
- Identification of Residues responsible for the Alkaline Bohr Effect in HaemoglobinNature, 1969
- Inhibition of CO2 Combination and Reduction of the Bohr Effect in Haemoglobin chemically modified at its α-Amino GroupsNature, 1969
- On the nature of allosteric transitions: A plausible modelJournal of Molecular Biology, 1965
- Hemoglobin and MyoglobinAdvances in Protein Chemistry, 1964
- Heme ProteinsAdvances in Protein Chemistry, 1948