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Purification and characterization of a novel anticoagulant peptide from marine echiuroid worm, Urechis unicinctus

Paper ID Volume ID Publish Year Pages File Format Full-Text
35590 45097 2008 6 PDF Available
Title
Purification and characterization of a novel anticoagulant peptide from marine echiuroid worm, Urechis unicinctus
Abstract

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: 3344 Da) 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 biochemical properties and health benefits of a novel nutraceutical or pharmaceutical material with an anticoagulant activity.

Keywords
Echiuroid worm; Urechis unicinctus; Anticoagulant peptide; Activated partial thromboplastin time (APTT); Surface plasmon resonance (SPR); Activated factor IX (FIXa)
First Page Preview
Purification and characterization of a novel anticoagulant peptide from marine echiuroid worm, Urechis unicinctus
Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 43, Issue 2, February 2008, Pages 179–184
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering