Hemoglobin providence. Functional consequences of two alterations of the 2,3-diphosphoglycerate binding site at position beta 82.
Open Access
- 1 December 1976
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 251 (23) , 7563-7571
- https://doi.org/10.1016/s0021-9258(17)32888-0
Abstract
No abstract availableThis publication has 35 references indexed in Scilit:
- Haemoglobin Rahere (beta Lys-Thr): A new high affinity haemoglobin associated with decreased 2, 3-diphosphoglycerate binding and relative polycythaemia.BMJ, 1975
- Functional properties of carboxypeptidase-digested hemoglobinsJournal of Molecular Biology, 1974
- Analysis of oxygen equilibrium of hemoglobin and control mechanism of organic phosphatesBiochemistry, 1973
- Stereochemistry of Cooperative Effects in Haemoglobin: Haem–Haem Interaction and the Problem of AllosteryNature, 1970
- Reactions of Haemoglobin Dimers after Ligand DissociationNature, 1970
- The interaction of 2,3-diphosphoglycerate with various human hemoglobinsJournal of Clinical Investigation, 1970
- Oxygenation of hemoglobin in the presence of 2,3-diphosphoglycerate. Effect of temperature, pH, ionic strength, and hemoglobin concentrationBiochemistry, 1969
- DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS*Annals of the New York Academy of Sciences, 1964
- DISC ELECTROPHORESIS‐I BACKGROUND AND THEORY*Annals of the New York Academy of Sciences, 1964
- SULFHYDRYL GROUPS AND THE STRUCTURE OF HEMOGLOBINThe Journal of general physiology, 1956