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

被引：53

作者：

Jo, Hee-Yeon ^{[1
]}

Jung, Won-Kyo ^{[2
]}

Kim, Se-Kwon ^{[1
,2
]}

机构：

[1] Pukyong Natl Univ, Dept Chem, Pusan 608737, South Korea

[2] Pukyong Natl Univ, Marine Bioproc Res Ctr, Pusan 608737, South Korea

来源：

PROCESS BIOCHEMISTRY | 2008年 / 43卷 / 02期

关键词：

echiuroid worm; Urechis unicinctus; anticoagulant peptide; activated partial thromboplastin time (APTT); surface plasmon resonance (SPR); activated factor IX (FIXa);

D O I：

10.1016/j.procbio.2007.11.011

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

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 (M-w: 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 GC(50) = 42.6 mu g 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. (c) 2007 Elsevier Ltd. All rights reserved.

引用

页码：179 / 184

页数：6

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