The effect of pH on the rate of dissociation of the oxygenated beta chain tetramer of Hb A
- 1 February 1983
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 111 (1) , 55-60
- https://doi.org/10.1016/s0006-291x(83)80116-8
Abstract
No abstract availableThis publication has 13 references indexed in Scilit:
- Heterotropic interactions in monomeric βSH chains from human hemoglobinArchives of Biochemistry and Biophysics, 1981
- Post-translational control of human hemoglobin synthesis The role of the differential affinity between globin chains in the control of mutated globin gene expressionBiochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1980
- Competition of normal β chains and sickle haemoglobin β chains for α chains as a post-translational control mechanismNature, 1978
- The oxygen affinity of hemoglobin βSH chains is concentration dependentBiochemical and Biophysical Research Communications, 1978
- Self-association of hemoglobin β SH chains is linked to oxygenationProceedings of the National Academy of Sciences, 1978
- 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
- Differences in Affinity of Variant β Chains for a Chains: A Possible Explanation for the Variation in the Percentages of β Chain Variants in HeterozygotesHemoglobin, 1977
- Aggregation of deoxyhemoglobin subunitsJournal of Biological Chemistry, 1976
- Tetramer-dimer dissociation in homoglobin and the Bohr effect.Journal of Biological Chemistry, 1976
- The properties and interactions of the isolated α- and β-chains of human haemoglobinJournal of Molecular Biology, 1966