Oxygen-linked CO2 binding to isolated beta subunits of human hemoglobin.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference37 articles.
1. The carbon dioxide affinity of various human hemoglobins.
2. Identification of the high and low affinity CO2-binding sites of human haemoglobin
3. Carbon 13 resonances of 13CO2 carbamino adducts of alpha and beta chains in human adult hemoglobin.
4. Oxygen Equilibrium and Kinetics of Isolated Subunits from Hemoglobin Kansas
5. Allosteric interactions in non-alpha chains isolated from normal human hemoglobin, fetal hemoglobin, and hemoglobin Abruzzo (beta143 (H21) His replaced by Arg)
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2. Interaction of allosteric effectors (ATP, CO2, H+) modulating oxygen affinity of the hemoglobin in the carp,Cyprinus carpio, in vitro;Journal of Comparative Physiology B;1989
3. Analysis of oxygen binding to Panulirus japonicus hemocyanin. The effect of divalent cations on the allosteric transition;European Journal of Biochemistry;1986-01
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