Rapid molecular characterization of mutations leading to unstable hemoglobin β-chain variants
- 1 October 1992
- journal article
- case report
- Published by Springer Nature in Annals of Hematology
- Vol. 65 (4) , 188-192
- https://doi.org/10.1007/bf01703113
Abstract
Characterization of unstable hemoglobins by protein analysis is often difficult. However, it is facilitated by DNA analysis, especially in the case of hyperunstable β-chain variants, which produce a β-thalassemia phenotype. We have applied an efficient strategy to the detection of such variants at the DNA level, based on computer-designed denaturing gradient gel electrophoresis (DGGE) of amplified DNA fragments. This approach makes it possible to detect any anomaly in the β-globin gene. We describe the use of the DGGE method for rapid characterization of β-chain variants and report a new missense mutation in the β-globin gene third exon, β 127 CAG-CGG/Gln-Arg, which is responsible for the synthesis of a highly unstable hemoglobin.Keywords
This publication has 40 references indexed in Scilit:
- Molecular characterization of cystic fibrosis: 16 Novel mutations identified by analysis of the whole cystic fibrosis conductance transmembrane regulator (CFTR) coding regions and splice site junctionsGenomics, 1992
- Dominant β‐thalassaemia trait in a Portuguese family is caused by a deletion of (G)TGGCTGGTGT(G) and an insertion of (G)GCAG(G) in codons 134, 135, 136 and 137 of the β‐globin geneBritish Journal of Haematology, 1991
- A SPONTANEOUS DELETION OF β33/34 Val IN EXON 2 OF THE β GLOBIN GENE (Hb KOREA) PRODUCES THE PHENOTYPE OF DOMINANT β THALASSAEMIABritish Journal of Haematology, 1991
- A New Strategy for Direct Detection of β‐Thalassemia MutationsAnnals of the New York Academy of Sciences, 1990
- Laron Dwarfism and Mutations of the Growth Hormone–Receptor GeneNew England Journal of Medicine, 1989
- Detection of polymorphisms of human DNA by gel electrophoresis as single-strand conformation polymorphisms.Proceedings of the National Academy of Sciences, 1989
- Hehoglobin Brest [β127(H5)Gln→LYS] a new Unstable Human Hemoglobin Variant Located at the α1β1 Interface with Specific Electrophoretic BehaviorHemoglobin, 1988
- Hb J-Antakya or α2β265(E9)Lys → Met in a Turkish family and Hb Complutense or α2β2127(H5)Gln → Glu in a Spanish family; correction of a previously published identificationBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1986
- Haemoglobin Perth: β32 (B14) Leu→Pro, An Unstable Haemoglobin Causing HaemolysisBritish Journal of Haematology, 1973
- Hemoglobin Abraham Lincoln, β32 (B14) Leucine → Proline AN UNSTABLE VARIANT PRODUCING SEVERE HEMOLYTIC DISEASEJournal of Clinical Investigation, 1973