The oxygen affinity of hemoglobin βSH chains is concentration dependent
- 30 September 1978
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 84 (4) , 852-857
- https://doi.org/10.1016/0006-291x(78)91662-5
Abstract
No abstract availableThis publication has 10 references indexed in Scilit:
- Self-association of hemoglobin β SH chains is linked to oxygenationProceedings of the National Academy of Sciences, 1978
- Oxygen-linked CO2 binding to isolated beta subunits of human hemoglobin.Journal of Biological Chemistry, 1977
- Thermodynamic studies on subunit assembly in human hemoglobin. Self-association of oxygenated chains (alphaSH and betaSH): determination of stoichiometries and equilibrium constants as a function of temperature.Journal of Biological Chemistry, 1977
- The Bohr effect of the isolated α and ß chains of human hemoglobinFEBS Letters, 1976
- Darwinian evolution in the genealogy of haemoglobinNature, 1975
- Homos and Heteros among the HemosScience, 1974
- Determination of oxygen equilibria with a versatile new tonometerAnalytical Biochemistry, 1965