Hb M Dothan [β 25/26 (B7/B8)/(GGT/GAG→GAG//Gly/Glu→Glu]; a new mechanism of unstable methemoglobin variant and molecular characteristics

Ferdane Kutlar, L. M. Hilliard, L. Zhuang, N. Patel, Binnur Eroglu, Steffen E Meiler, H. Carmichael, R. B. Russell, Abdullah Kutlar

Research output: Contribution to journalArticle

9 Scopus citations

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 languageEnglish (US)
Pages (from-to)235-238
Number of pages4
JournalBlood Cells, Molecules, and Diseases
Volume43
Issue number3
DOIs
Publication statusPublished - Nov 1 2009

    Fingerprint

Keywords

  • Amino acid deletion
  • Cyanosis
  • M-hemoglobin
  • Methemoglobin
  • Unstable beta chain variant

ASJC Scopus subject areas

  • Molecular Medicine
  • Molecular Biology
  • Hematology
  • Cell Biology

Cite this