The oxygen affinity of hemoglobin βSH chains is concentration dependent
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference9 articles.
1. Homos and Heteros among the Hemos
2. The Effect of pH on the Rates of Ligand Replacement Reactions of Human Adult and Fetal Hemoglobins and Their Subunits
3. The Bohr effect of the isolated α and ß chains of human hemoglobin
4. Allosteric interactions in non-alpha chains isolated from normal human hemoglobin, fetal hemoglobin, and hemoglobin Abruzzo (beta143 (H21) His replaced by Arg)
5. Oxygen-linked CO2 binding to isolated beta subunits of human hemoglobin.
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1. Deciphering the Molecular Code of Hemoglobin Allostery;Advances in Protein Chemistry;1998
2. Effects of NaCl on the linkages between O2 binding and subunit assembly in human hemoglobin: titration of the quaternary enhancement effect;Biophysical Chemistry;1997-02
3. Role of alpha and beta carboxyl-terminal residues in the kinetics of human oxyhemoglobin dimer assembly.;Journal of Biological Chemistry;1994-03
4. Functional consequences of mutations at the allosteric interface in hetero- and homo-hemoglobin tetramers;Protein Science;1993-08
5. Kinetics of oxygen binding and subunit assembly for the hemoglobin alpha subunit;Biophysical Chemistry;1992-05
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