Abstract
A new unstable β globin chain variant associated with methemoglobin (Met-Hb) phenotype was found in a Caucasian infant. Molecular analysis of the β globin gene using polymerase chain reaction (PCR) amplification and sequencing led to the detection of a new in frame deletion in exon-1. Direct sequencing of the PCR product revealed a 3 bp deletion (-GTG) between codons 25/26, which resulted in the loss of a single amino acid (-Gly). We propose that this newly discovered unstable M-hemoglobin (M-Hb) variant, named Hb Dothan [GGT/GAG→GAG//Gly/Glu→Glu], is caused by a shift in the amino acid sequence and altered packing of the B and E helices during β globin synthesis, and also changes the orientation of the critical proximal and distal histidine in the F and E helices respectively. Phenotype/Genotype features and molecular characteristics of this new beta chain are presented in this communication.
Original language | English (US) |
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Pages (from-to) | 235-238 |
Number of pages | 4 |
Journal | Blood Cells, Molecules, and Diseases |
Volume | 43 |
Issue number | 3 |
DOIs | |
State | Published - Nov 2009 |
Keywords
- Amino acid deletion
- Cyanosis
- M-hemoglobin
- Methemoglobin
- Unstable beta chain variant
ASJC Scopus subject areas
- Molecular Medicine
- Molecular Biology
- Hematology
- Cell Biology