Intramolecular crosslink of human hemoglobin with a long chain dicarboxylic acid between the α subunits

H. Kwansa, A. Razynska, J. H. Collins, E. Bucci

Research output: Contribution to journalArticle

Abstract

Crosslinks between the β82 lysines using 10, 12, and 14 carbon dicarboxylic acids is reported. It was found that the incubation mixture of human deoxyhemoglobin with bis- (3,5-dibromosalicyl)sebacate contains three main intramolecularly crosslinked molecular species. The major component is a hemoglobin crosslinked between the β82 lysines. These species have low oxygen affinity. Preliminary data suggest that the α subunits are crosslinked between the α99 residues.

Original languageEnglish (US)
JournalArtificial Cells, Blood Substitutes, and Biotechnology
Volume22
Issue number5
StatePublished - Nov 1994
Externally publishedYes

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Dicarboxylic Acids
Hemoglobin
Lysine
Hemoglobins
Carbon
Oxygen
Acids
bis(3,5-dibromosalicyl)sebacate
deoxyhemoglobin

ASJC Scopus subject areas

  • Biotechnology
  • Biomedical Engineering
  • Biomaterials
  • Hematology

Cite this

Intramolecular crosslink of human hemoglobin with a long chain dicarboxylic acid between the α subunits. / Kwansa, H.; Razynska, A.; Collins, J. H.; Bucci, E.

In: Artificial Cells, Blood Substitutes, and Biotechnology, Vol. 22, No. 5, 11.1994.

Research output: Contribution to journalArticle

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