Introduction of negative charges to a crosslinked hemoglobin: Lack of effect on plasma half time

Michelle Thomas, Barbara Matheson-Urbaitis, Herman Kwansa, Enrico Bucci, Clara Fronticelli

Research output: Contribution to journalArticle

Abstract

Intramolecularly crosslinked hemoglobins do not dissociate into α1β1 dimers. As a result, they escape glomerular filtration and have plasma half times of 4 hours. This value is shorter than for albumin (5.2 hours) with similar molecular weight but higher negative charge. The present study was done to determine if increased negative charge on a hemoglobin covalently crosslinked with bis (3,5-dibromosalicyl) sebacate would lengthen its plasma half time. Negative charge was introduced by acylation with succinic anhydride. The product had a higher negative charge; however, plasma half time was not increased. A larger fraction of the succinylated material was excreted in the urine suggesting molecular instability.

Original languageEnglish (US)
Pages (from-to)309-314
Number of pages6
JournalArtificial Cells, Blood Substitutes, and Immobilization Biotechnology
Volume25
Issue number3
DOIs
StatePublished - Jan 1 1997

ASJC Scopus subject areas

  • Biotechnology
  • Biomedical Engineering

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