Correlation Engine 2.0
Clear Search sequence regions

  • acetyl (1)
  • amino acid (1)
  • bohr effect (2)
  • cofactors (1)
  • globin (2)
  • haemoglobin (8)
  • humans (1)
  • impair (1)
  • ions (2)
  • native (1)
  • oxygen (2)
  • phosphates (2)
  • plasmid (1)
  • protons (1)
  • subunits (1)
  • suggest (1)
  • vertebrate (4)
  • α chain (1)
  • Sizes of these terms reflect their relevance to your search.

    In vertebrate haemoglobin (Hb), the NH2-terminal residues of the α- and β-chain subunits are thought to play an important role in the allosteric binding of protons (Bohr effect), CO2 (as carbamino derivatives), chloride ions, and organic phosphates. Accordingly, acetylation of the α- and/or β-chain NH2-termini may have significant effects on the oxygenation properties of Hb. Here we investigate the effect of NH2-terminal acetylation by using a newly developed expression plasmid system that enables us to compare recombinantly expressed Hbs that are structurally identical except for the presence or absence of NH2-terminal acetyl groups. Experiments with native and recombinant Hbs of representative vertebrates reveal that NH2-terminal acetylation does not impair the Bohr effect, nor does it significantly diminish responsiveness to allosteric cofactors, such as chloride ions or organic phosphates. These results suggest that observed variation in the oxygenation properties of vertebrate Hbs is principally explained by amino acid divergence in the constituent globin chains rather than post-translational modifications of the globin chain NH2-termini. © 2020 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society.


    Chandrasekhar Natarajan, Anthony V Signore, Vikas Kumar, Roy E Weber, Angela Fago, Jay F Storz. Effect of NH2-terminal acetylation on the oxygenation properties of vertebrate haemoglobin. The Biochemical journal. 2020 Oct 16;477(19):3839-3850

    Expand section icon Mesh Tags

    Expand section icon Substances

    PMID: 32936244

    View Full Text