Functional studies of the double mutant hemoglobin Stanleyville II/S α278 Lys β26 Val: Identification of a site of intermolecular contact on the α chain
- 1 August 1977
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 77 (3) , 1108-1117
- https://doi.org/10.1016/s0006-291x(77)80093-4
Abstract
No abstract availableThis publication has 19 references indexed in Scilit:
- Hemoglobin Dakar Hb Grady: Demonstration by a new approach to the analysis of the tryptic core region of the α chain and oxygen equilibrium propertiesBiochimica et Biophysica Acta (BBA) - Protein Structure, 1976
- α-Chain contacts in the polymerization of sickle haemoglobinNature, 1976
- Hemoglobin C Ziguinchor αA2β62 (A3)Glu → Val β58(E2)→ Arg: The second sickling variant with amino acid substitutions in 2 residues of the β polypeptide chainFEBS Letters, 1975
- Role of hybrid tetramer formation in gelation of haemoglobin SNature, 1975
- The Concentration Dependence of the Oxygen Affinity of Haemoglobin SBritish Journal of Haematology, 1975
- Interaction entre les hémoglobines Stanleyville II et S dans une famille du Zaïre. Etude de l'hybride Stanleyville II/S (α278 lys β26 val)Biochimie, 1973
- Ligand-induced conformational dependence of hemoglobin in sickling interactionsJournal of Molecular Biology, 1971
- Stereochemistry of Cooperative Effects in Haemoglobin: Haem–Haem Interaction and the Problem of AllosteryNature, 1970
- Studies on the heterogeneity of hemoglobinJournal of Chromatography A, 1965
- Homozygous Sickle-cell Anaemia Arising from two Different Haemoglobins SBMJ, 1964