Single Chain Alkali Resistance in Hemoglobin Rainier: β 145 Tyrosine → Histidine
- 21 November 1969
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 166 (3908) , 1005-1006
- https://doi.org/10.1126/science.166.3908.1005
Abstract
The mechanism of alkali resistance in hemoglobin Rainier, an adult human hemoglobin variant (beta 145 tyrosinie --> histidinie), has been investigated. Alkali denaturation kinetics, electrophoretic and hybridization study. and ultracentrifuge analysis provided evidence for a monomeric beta Rainiier chain resisting denaturation at alkaline pH. These data provide evidence for a previously unrecognized effect of a single amino acid substitution, that is, the change of the alkali denaturation properties of monomneric chains.Keywords
This publication has 7 references indexed in Scilit:
- Molecular Pathology of Human HaemoglobinNature, 1968
- Hemoglobin Rainier (β 145 Tyrosine → Histidine): Alkali-Resistant Hemoglobin with Increased Oxygen AffinityScience, 1968
- On the mechanism of the dissociation of haemoglobinJournal of Molecular Biology, 1967
- Protein-protein interaction among hemoglobin subunitsArchives of Biochemistry and Biophysics, 1967
- The Preparation and Properties of the Isolated α and β Subunits of Hemoglobin A*Biochemistry, 1966
- Chemical Characterization and Subunit Hybridization of Human Hemoglobin H and Associated Compounds*Biochemistry, 1963
- Carbon-14 Labelled Hybrids of HæmoglobinNature, 1960