Structural study of hemoglobin Knossos, β27 (B9) Ala→Ser A new abnormal hemoglobin present as a silent β-thalassemia
| Autor: | Yves Blouquit, M. Boussiou, Nicole Arous, Frédéric Galactéros, Phaedon Fessas, Dimitris Loukopoulos, M. Sellaye, George Komis, Jean-Philippe Rosa |
|---|---|
| Jazyk: | angličtina |
| Předmět: |
chemistry.chemical_classification
Isoelectric focusing Thalassemia Biophysics Hemoglobin variants Peptide Cell Biology medicine.disease Urea—Triton—acrylamide electrophoresis Biochemistry Phenotype Molecular biology Abnormal hemoglobin Neutral substitution β Thalassemia intermedia Hemoglobin A chemistry Structural Biology hemic and lymphatic diseases Genetics medicine Silent β thallasemia trait Molecular Biology Hemoglobin Knossos |
| Zdroj: | FEBS Letters. (2):247-250 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/0014-5793(82)81052-1 |
| Popis: | A new electrophoretically silent hemoglobin variant is described that produces the classical phenotype of β thalassemic intermedia in association with β° thalassemia trait. This variant has the expression of a silent β thalassemia trait. The abnormal hemoglobin was detected by acid—urea—Triton—acrylamide electrophoresis and further demonstrated by isoelectric focusing. The amount of the variant in carrier is ∼30% of the total hemoglobin. No instability was found. Absence of hemoglobin A in the propositus blood facilitated structural studies. Peptides maps were normal but analysis of individual peptide spots showed an Ala→Ser substitution in the βT3. This variant has been previously called Hb Knossos (β27 (B9) Ala→Ser). |
| Databáze: | OpenAIRE |
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