Thermodynamic characterization of subunit association in liganded ferrohemoglobin. The temperature pH, and anion dependence of the carboxyhemoglobin A dimer-tetramer equilibrium.-Reference-Cited by-同舟云学术

Thermodynamic characterization of subunit association in liganded ferrohemoglobin. The temperature pH, and anion dependence of the carboxyhemoglobin A dimer-tetramer equilibrium.

Published:1978-07 Issue:14 Volume:253 Page:4881-4885
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Barksdale A.D.,Rosenberg A.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference27 articles.

1. Relation between allosteric effects and changes in the energy of bonding between molecular subunits

2. Thermodynamic studies on subunit assembly in human hemoglobin. Temperature dependence of the dimer-tetramer association constants for oxygenated and unliganded hemoglobins.

3. Linked Functions and Reciprocal Effects in Hemoglobin: A Second Look

4. INTERACTION OF HAEMOGLOBIN WITH PROTONS, CO2 AND 2,3-DIPHOSPHOGLYCERATE

5. Oxygenation-linked subunit interactions in human hemoglobin: experimental studies on the concentration dependence of oxygenation curves

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