Functional properties of hemoglobins intramolecularly crosslinked with tricarboxylic and dicarboxylic acids

E. Bucci, A. Razynska, H. Kwansa, C. Fronticelli

Research output: Contribution to journalConference articlepeer-review

2 Scopus citations

Abstract

The paper discusses the functional properties of hemoglobins intramolecularly crosslinked with tricarboxylic and dicarboxylic acids. Intramolecular crosslinks are produced either between the α99 or β82 lysines. The increasing length of the crosslink between the β subunits from 4 to 14 carbon atoms progressively decreases the oxygen affinity of hemoglobin. Preliminary data suggest that the same may be true for the crosslinks between α subunits. The triester of benzene-tricarboxylic acid produces very homogeneous β-β crosslinked hemoglobins, with low oxygen affinity.

Original languageEnglish (US)
Pages (from-to)A84
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 'Functional properties of hemoglobins intramolecularly crosslinked with tricarboxylic and dicarboxylic acids'. Together they form a unique fingerprint.

Cite this