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Purification and Characterization of a Novel Anticoagulant Peptide from Marine Echiuroid Worm, Urechis unicinctus

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영어

A novel inhibitory peptide against blood coagulation factor IXa (FIXa) was isolated from the marine echiuroid worm (Urechis unicinctus, order Urechidae). U. unicinctus anticoagulant peptide (UAP), GELTPESGPDLFVHFLDGNPSYSLYADAVPR (Mw: 3343 kDa) potently prolonged the activated partial thromboplastin time (APTT), corresponding to inhibition of an endogenous blood coagulation factor in the intrinsic pathway. In the specific factor inhibitory assay, FIXa activity in normal plasma was significantly (P<0.05) decreased by addition of UAP in dose-dependant manner (IC50 = 42.6 μg ml-1). Binding affinity assay using a surface plasmon resonance (SPR) spectrometer showed that UAP binding to FIXa could inhibit the interaction between FIXa and FX. The present results suggest that UAP bound to FIXa prolongs blood clotting time by inhibiting the conversion of FX to FXa in the intrinsic tenase complex. It is possible to provide biochemicalproperties and health benefits of a novel nutraceutical or pharmaceutical material with an anticoagulant activity.

저자정보

  • Won-Kyo Jung Marine Bioprocess Research Center, Pukyong National University
  • Hee-Yeon Jo Department of Chemistry, Pukyong National University
  • Se-Kwon Kim Marine Bioprocess Research Center, Pukyong National University, Department of Chemistry, Pukyong National University

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