Hemoglobin Rainier (β 145 Tyrosine → Histidine): Alkali-Resistant Hemoglobin with Increased Oxygen Affinity
- 16 February 1968
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 159 (3816) , 741-743
- https://doi.org/10.1126/science.159.3816.741
Abstract
Hemoglobin Rainier, a new hemoglobin variant associated with erythrocytosis, was found in six members of a Caucasiant family. Structurally, it represents substitution of histidine for the invariant residute H23 tyrosine in the β-hemoglobin polypeptide chain (β145 tyrosine → histidine). Hemoglobin Rainier is the first example of a single amino acid substitution in adult human hemoglobin, causing increased resistance to alkali denaturation.This publication has 14 references indexed in Scilit:
- Hemoglobin Yakima: I. Clinical and Biochemical Studies*Journal of Clinical Investigation, 1967
- Oxygen Binding by Haemoglobin J-Cape Town (α2 92 Arg → Gln)Nature, 1967
- Abnormal human haemoglobins: Separation and characterization of the α and β chains by chromatography, and the determination of two new variants, Hb chesapeake and Hb J (Bangkok)Journal of Molecular Biology, 1966
- Polycythemia associated with a hemoglobinopathy.Journal of Clinical Investigation, 1966
- Structure and function of haemoglobinJournal of Molecular Biology, 1965
- Structure and function of haemoglobinJournal of Molecular Biology, 1965
- Structural Studies of Aminoethylated Hemoglobins by Automatic Peptide ChromatographyCold Spring Harbor Symposia on Quantitative Biology, 1964
- On the recombination of canine and human haemoglobinsJournal of Molecular Biology, 1962
- A Hæmoglobin with Unusual Alkaline-denaturation Properties in a Turkish-Cypriot WomanNature, 1959
- Studies on the structure of hemoglobin I. Physicochemical properties of human globinBiochimica et Biophysica Acta, 1958