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 language | English (US) |
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Pages (from-to) | 36-41 |
Number of pages | 6 |
Journal | BBA - Gene Structure and Expression |
Volume | 951 |
Issue number | 1 |
DOIs | |
State | Published - Nov 10 1988 |
Keywords
- Gene amplification
- HPLC
- Mutation
- Synthetic oligonucleotide
ASJC Scopus subject areas
- Structural Biology
- Biophysics
- Biochemistry
- Genetics