期刊
FOOD CHEMISTRY
卷 117, 期 4, 页码 687-692出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2009.04.077
关键词
Blue mussel; Mytilus edulis; Anticoagulant peptide; Blood clotting time; Prothrombinase complex; Intrinsic tenase complex
资金
- Ministry of Land, Transport and Maritime, Republic of Korea
- Chosun University
- Korea Institute of Marine Science & Technology Promotion (KIMST) [B10400107A280000100] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
- National Research Foundation of Korea [핵09B2519] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
A potent anticoagulant oligopeptide was isolated from the edible parts of blue mussel (Mytilus edulis). M. edulis anticoagulant peptide (MEAP) with an approximately 2.5 kDa molecular mass was similar to the amino acid sequence of the EF-hand domain of calmodulin from scallop adductor muscle. MEAP could potently prolong both the thrombin time and the activated partial thromboplastin time, and specifically interact with blood coagulation factors: FIX, FX, and FII. MEAP could inhibit proteolytic activation of FX by the intrinsic FXase and formation of FIIa by a prothrombinase complex in dose-dependant reactions. This study elucidated that MEAP prolonged blood clotting by inhibiting activation of FX in the intrinsic tenase complex (FIXa/VIIIa/PLs) and conversion of FII to FIIa in the prothrombinase complex (FXa/FVa/PLs). (c) 2009 Elsevier Ltd. All rights reserved.
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