The effects of 2,3-diphosphoglycerate on native and chemically modified horse hemoglobin
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(71)80262-4/fullpdf
Reference18 articles.
1. The effect of organic phosphates from the human erythrocyte on the allosteric properties of hemoglobin
2. Effect of organic and inorganic phosphates on the oxygen equilibrium of human erythrocytes
3. Reciprocal binding of oxygen and diphosphoglycerate by human hemoglobin.
4. Binding of 2,3-Diphosphoglycerate and Adenosine Triphosphate to Human Haemoglobin A
5. Binding of 2,3-diphosphoglycerate to oxyhemoglobin
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2. The influence of protons and salts on the reactivity of hemoglobin with oxygen;International Journal of Quantum Chemistry;2009-06-18
3. Comparative study of the oxyhaemoglobin dissociation curve of four mammals: Man, dog, horse and cattle;Comparative Biochemistry and Physiology Part A: Physiology;1993-12
4. Hemoglobin and Myoglobin Ligand Kinetics;Annual Review of Physical Chemistry;1979-10
5. 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 Changeux;Biochemistry;1973-02-27
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