Hb Natal or α2(minus Tyr-Arg)β2: A high oxygen affinity α chain variant with a deleted carboxy-terminus resulting from a TAC → TAA (Tyr → terminating codon) mutation in codon α140

V. B. Jogessar, K. Westermeyer, B. B. Webber, J. B. Wilson, H. Hu, J. M. Gonzalez-Redondo, A. Kutlar, T. H.J. Huisman

Research output: Contribution to journalArticle

13 Scopus citations

Abstract

The discovery is reported of a fast-moving α chain variant (Hb Natal) which is characterized by a shortened α polypeptide chain because of the deletion of the Tyr-Arg carboxy-terminal residues. Through amplification of appropriate segments of DNA and hybridization with synthetic oligonucleotide probes, it was possible to detect a C → A mutation in codon 140 of the α2 globin gene, which causes a change in the codon for tyrosine to a terminating codon. Hb Natal or α2(minus Tyr-Arg)β2 has a high affinity for oxygen without a Bohr effect and heme-heme interaction. These results provide direct evidence for the importance of the tyrosine residue at α140 in the oxygenation-deoxygenation process.

Original languageEnglish (US)
Pages (from-to)36-41
Number of pages6
JournalBBA - Gene Structure and Expression
Volume951
Issue number1
DOIs
StatePublished - Nov 10 1988

Keywords

  • Gene amplification
  • HPLC
  • Mutation
  • Synthetic oligonucleotide

ASJC Scopus subject areas

  • Structural Biology
  • Biophysics
  • Biochemistry
  • Genetics

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