A possible new mechanism of oxygen affinity modulation in mammalian hemoglobins

Research output: Contribution to journalArticlepeer-review

Abstract

Bovine red cells do not contain appreciable amounts of 2,3-diphosphoglycerate (2,3-DPG). Bovine hemoglobin, however, has a particular sensitivity to chloride ions and as a result it can attain oxygen affinity values lower than those measured for human hemoglobin in the presence of 2,3-DPG. The interaction of bovine hemoglobin with anions is modulated by the hydrophobic characteristics of the protein. Comparison of the hydropathy plots of primate and ruminant hemoglobins indicates constant regions of opposite hydrophobicity, which have fixed amino acid differences. A model is proposed for explaining the regulation of oxygen affinity by chlorides, as an alternative to the classic modulation by 2,3-DPG.

Original languageEnglish (US)
Pages (from-to)141-146
Number of pages6
JournalBiophysical Chemistry
Volume37
Issue number1-3
DOIs
StatePublished - Aug 31 1990
Externally publishedYes

Keywords

  • Binding mechanism
  • Chloride
  • Diphosphoglycerate
  • Hemoglobin
  • Oxygen affinity

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Organic Chemistry

Fingerprint

Dive into the research topics of 'A possible new mechanism of oxygen affinity modulation in mammalian hemoglobins'. Together they form a unique fingerprint.

Cite this