Abstract
We have characterized the structural abnormality of a new alpha chain mutant found in a Kurdish; family. The clinical and hematological investigation of eight individuals have shown that the a variant is associated with a beta degrees-thalassemia mutation (nonsense codon 39). The tryptic peptide map and sequencing of the abnormal peptide revealed the substitution of an aspartic acid by a tyrosine residue at position 47 of the alpha chain; furthermore, selective amplification and molecular analysis of both alpha genes have assigned the new mutation to the alpha 2 gene. The variant, named Hb Kurdistan, is clinically silent but the percentage of this hemoglobin found in the only double heterozygote for beta degrees-thalassemia and alpha-Kurdistan, presumably indicates a lower affinity of the abnormal chain for the beta polypeptides.
Original language | English |
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Pages (from-to) | 11-18 |
Number of pages | 8 |
Journal | Hemoglobin |
Volume | 18 |
Issue number | 1 |
Publication status | Published - 1994 |
Keywords
- HEMOGLOBINS
- CELLS
- DNA