Heparinase I acts on a synthetic heparin pentasaccharide corresponding to the antithrombin III binding site

Guangli Yu, Laurie LeBrun, Nur Sibel Gunay, Debra Hoppensteadt, Jeanine M. Walenga, Jawed Fareed, Robert J. Linhardt

Research output: Contribution to journalArticlepeer-review

45 Scopus citations

Abstract

A synthetic pentasaccharide, containing an intact antithrombin III (ATIII) binding site that is in clinical studies a specific antifactor Xa agent, serves as a substrate for a heparin lyase (heparinase I, EC 4.2.2.7) from Flavobacterium heparinum. Heparinase I, currently being assessed as a heparin reversal agent, also reverses the antifactor Xa activity of this synthetic pentasaccharide by breaking it down to inactive disaccharide and trisaccharide products.

Original languageEnglish
Pages (from-to)549-556
Number of pages8
JournalThrombosis Research
Volume100
Issue number6
DOIs
StatePublished - 15 Dec 2000
Externally publishedYes

Keywords

  • Heparin lyase
  • Heparinase
  • Neutralization
  • Pentasaccharide
  • Reversal

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