Structural features and anticoagulant activities of a novel natural low molecular weight heparin from the shrimp Penaeus brasiliensis

Biochim Biophys Acta. 1999 Aug 5;1428(2-3):273-83. doi: 10.1016/s0304-4165(99)00087-2.

Abstract

A natural low molecular weight heparin (8.5 kDa), with an anticoagulant activity of 95 IU/mg by the USP assay, was isolated from the shrimp Penaeus brasiliensis. The crustacean heparin was susceptible to both heparinase and heparitinase II from Flavobacterium heparinum forming tri- and di-sulfated disaccharides as the mammalian heparins. (13)C and (1)H NMR spectroscopy revealed that the shrimp heparin was enriched in both glucuronic and non-sulfated iduronic acid residues. The in vitro anticlotting activities in different steps of the coagulation cascade have shown that its anticoagulant action is mainly exerted through the inhibition of factor Xa and heparin cofactor II-mediated inhibition of thrombin. The shrimp heparin has also a potent in vivo antithrombotic activity comparable to the mammalian low molecular weight heparins.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antithrombins / chemistry
  • Antithrombins / isolation & purification*
  • Cattle
  • Chromatography, High Pressure Liquid
  • Chromatography, Paper
  • Electrophoresis, Agar Gel
  • Glucuronates / analysis
  • Glucuronic Acid
  • Heparin Lyase
  • Heparin, Low-Molecular-Weight / chemistry
  • Heparin, Low-Molecular-Weight / isolation & purification*
  • Iduronic Acid / analysis
  • Magnetic Resonance Spectroscopy / methods
  • Molecular Weight
  • Penaeidae / metabolism*
  • Peptide Fragments / chemistry
  • Polysaccharide-Lyases

Substances

  • Antithrombins
  • Glucuronates
  • Heparin, Low-Molecular-Weight
  • Peptide Fragments
  • Iduronic Acid
  • Glucuronic Acid
  • Polysaccharide-Lyases
  • Heparin Lyase
  • heparitinsulfate lyase