A Calorimetric Study of the CO Bohr Effect of Monomeric Haemoglobins
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1976.tb10192.x/fullpdf
Reference11 articles.
1. Die O2-Bindungseigenschaften einiger Larvalhamoglobine von Chironomus th. thummi
2. Heterotropic Allosterism of Monomeric Haemoglobins of Chironomus thummi thummi
3. Linked Functions and Reciprocal Effects in Hemoglobin: A Second Look
4. Ligand-Specific Bohr Effect in Haemoglobins
5. The Bohr Proton-Binding Site in a Monomeric Haemoglobin. A Nuclear-Magnetic-Resonance Study
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1. Resonance Raman study of deoxy and ligated (O2 and CO) mesoheme IX-reconstituted myoglobin, hemoglobin and its α and β subunits;Journal of Inorganic Biochemistry;2004-09
2. Dynamic properties of monomeric insect erythrocruorin III from Chironomus thummi-thummi: relationships between structural flexibility and functional complexity;Biophysical Journal;1997-11
3. Solution NMR Study of the Structural Basis of the Bohr Effect in the Monomeric Hemoglobins from Chironomus thummi thummi;Biochemistry;1997-02-01
4. Solution 1H-NMR Structure of the Heme Cavity in the Low-Affinity State for the Allosteric Monomeric Cyano-Met Hemoglobins from Chironomus thummi thummi. Comparison to the Crystal Structure;European Journal of Biochemistry;1996-05
5. [7] Preparation and characterization of insect hemoglobins from Chironomus thummi thummi;Hemoglobins Part B: Biochemical and Analytical Methods;1994
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