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 Biotechnology
Volume25
Issue number3
StatePublished - May 1997
Externally publishedYes

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Hemoglobin
Hemoglobins
Plasmas
Acylation
Dimers
Albumins
Molecular Weight
Molecular weight
Urine

ASJC Scopus subject areas

  • Biomedical Engineering
  • Hematology
  • Biotechnology
  • Biomaterials

Cite this

Introduction of negative charges to a crosslinked hemoglobin : Lack of effect on plasma half time. / Thomas, Michelle; Matheson-Urbaitis, Barbara; Kwansa, Herman; Bucci, Enrico; Fronticelli, Clara.

In: Artificial Cells, Blood Substitutes, and Biotechnology, Vol. 25, No. 3, 05.1997, p. 309-314.

Research output: Contribution to journalArticle

Thomas, Michelle ; Matheson-Urbaitis, Barbara ; Kwansa, Herman ; Bucci, Enrico ; Fronticelli, Clara. / Introduction of negative charges to a crosslinked hemoglobin : Lack of effect on plasma half time. In: Artificial Cells, Blood Substitutes, and Biotechnology. 1997 ; Vol. 25, No. 3. pp. 309-314.
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