Bovine hemoglobin as a potential source of hemoglobin-based oxygen carriers: crosslinking with bis(2,3-dibromosalycyl)fumarate

Clara Fronticelli, Toshihide Sato, Charles Orth, Enrico Bucci

Research output: Contribution to journalArticle

Abstract

Reaction in anaerobic conditions of bovine hemoglobin with bis(2,3-dibromosalycyl)fumarate resulted in new derivatives with p50 in excess of 40 mmHg, as determined at 37°C in 0.15 M Cl- at pH 7.4. Although the chromatographic preparations indicated some heterogeneity of the reacted material, the proteins obtained were homogeneous with regard to sedimentation velocity, which showed the presence of only nondissociable tetrameric species. SDS gel electrophoresis showed the presence of a new band with a mobility corresponding approximately to a molecular mass of 32 kDa, indicating the presence of covalent intramolecular crosslinks between subunit pairs. Chromatographic analyses indicated that both α and β chains were chemically modified. The retention times in rats of the crosslinked hemoglobin was 10-times longer than that of untreated hemoglobin.

Original languageEnglish (US)
Pages (from-to)76-81
Number of pages6
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume874
Issue number1
DOIs
StatePublished - Nov 7 1986
Externally publishedYes

Keywords

  • Bis(2,3-dibromosalycyl)fumarate
  • Crosslinking
  • Hemoglobin
  • Oxygen retention
  • Retention time

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology

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