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 journalConference articlepeer-review

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)
Pages (from-to)A122
JournalArtificial Cells, Blood Substitutes, and Immobilization Biotechnology
Volume22
Issue number5
StatePublished - Nov 1 1994
EventProceedings of the 11th Congress of the International Society for Artificial Cells, Blood Substitutes and Immobilization Biotechnology, (ISABI) - Boston, MA, USA
Duration: Jul 24 1994Jul 27 1994

ASJC Scopus subject areas

  • Biotechnology
  • Biomedical Engineering

Fingerprint

Dive into the research topics of 'Intramolecular crosslink of human hemoglobin with a long chain dicarboxylic acid between the α subunits'. Together they form a unique fingerprint.

Cite this