Immobilized hemoglobin in the purification of hemoglobin-based oxygen carriers

Emilia Chiancone, Clara Fronticelli, Maurizio Gattoni, Barbara K. Urbaitis, Enrico Bucci

Research output: Contribution to journalArticlepeer-review

Abstract

Chemically modified hemoglobins can be used as oxygen carriers in cell-free fluids provided that they have a low oxygen affinity and are stable towards dissociation into subunits. The latter species, are undesirable because they are filtered rapidly through the kidneys, have renal toxicity and are characterized by a high oxygen affinity. A most important step in the preparation of hemoglobin-based oxygen carriers is therefore their purification from any dissociable material. Hemoglobin immobilized as αβ dimers on Sepharose lends itself naturally to this purpose as it is able to interact in a specific and reversible way with soluble αβ dimers. Hemoglobin affinity columns are very effective in the purification of cross-linked and pseudo-cross-linked human and bovine hemoglobin. The applicability of the technique is enhanced by the ease with which αβ dimers from different species cross-interact to yield hybrid α2β2 tetramers. It is shown that hemoglobin affinity columns may provide analytical information on the cross-linking reaction itself.

Original languageEnglish (US)
Pages (from-to)117-123
Number of pages7
JournalJournal of Chromatography A
Volume604
Issue number1
DOIs
StatePublished - Jun 26 1992
Externally publishedYes

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry
  • Organic Chemistry

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