Properties of chemically modified Ni(II)Fe(II) hybrid hemoglobins
- 1 November 1986
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 192 (2) , 331-336
- https://doi.org/10.1016/0022-2836(86)90368-2
Abstract
No abstract availableThis publication has 27 references indexed in Scilit:
- Correlation between the iron-histidine stretching frequencies and oxygen affinity of hemoglobins. A continuous strain modelJournal of the American Chemical Society, 1985
- The Monod-Wyman-Changeux allosteric model describes haemoglobin oxygenation with only one adjustable parameterJournal of Molecular Biology, 1983
- Close correlation between Monod-Wyman-Changeux parameters, L and c, and its implication for the stereochemical mechanism of haemoglobin allosteryJournal of Molecular Biology, 1981
- Role of Bohr group salt bridges in cooperativity in hemoglobinBiochimica et Biophysica Acta (BBA) - Protein Structure, 1978
- Allosteric effects in cobaltohaemoglobin as studied by precise oxygen equilibrium measurementsJournal of Molecular Biology, 1977
- Structure and function of haemoglobinProgress in Biophysics and Molecular Biology, 1976
- Alteration of functional properties associated with the change in quaternary structure in unliganded haemoglobinJournal of Molecular Biology, 1975
- The binding of carbon dioxide by horse haemoglobinBiochemical Journal, 1971
- Studies on the function of abnormal hemoglobins I. An improved method for automatic measurement of the oxygen equilibrium curve of hemoglobinBiochimica et Biophysica Acta (BBA) - Protein Structure, 1970
- The Chemistry of the Bohr EffectJournal of Biological Chemistry, 1961