Hemoglobin Sunshine Seth - α2(94 (G1) Asp→His)β2
- 1 January 1979
- journal article
- research article
- Published by Taylor & Francis in Hemoglobin
- Vol. 3 (2-3) , 145-159
- https://doi.org/10.3109/03630267908998910
Abstract
Hemoglobin Sunshine Seth in which a histidyl is substituted for an aspartyl residue at position 94 of the α chain was detected at birth in a Caucasian male infant during cord blood screening and is present also in the mother and a male sibling. Although the substitution is in the α1β2 contact, it is without obvious deleterious effect on the hematological parameters or the health of the affected individuals.This publication has 15 references indexed in Scilit:
- Measuring Relative Electrophoretic Mobilities of Mutant Hemoglos and Globin ChainsHemoglobin, 1978
- The structure of horse methaemoglobin at 2.0 Å resolutionJournal of Molecular Biology, 1977
- Separation of Human Hemoglobins by Deae-Cellulose Chromatography using Glycine-Kcn-Nacl DevelopersHemoglobin, 1976
- Three-dimensional fourier synthesis of human deoxyhaemoglobin at 2·5 Å resolution: Refinement of the atomic modelJournal of Molecular Biology, 1975
- Haemoglobin titusville: α94 Asp → AsnBiochimica et Biophysica Acta (BBA) - Protein Structure, 1975
- On the structure of the hemoglobins A, A2, and F in a Negro with homozygous β-thalassemiaBiochemical Medicine, 1974
- Hb Setif: G1 (94)α Asp → Tyr a new α chain hemoglobin variant with substitution of the residue involved in a hydrogen bond between unlike subunitsFEBS Letters, 1972
- An improved method for quantitative determination of human fetal hemoglobinAnalytical Biochemistry, 1970
- 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
- Preferential Release of Aspartic Acid During the Hydrolysis of ProteinsNature, 1950