A novel high molecular weight metalloproteinase cleaves fragment F1 of activated human prothrombin. |
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Authors: | Run-Qiang Chen Yang Jin Jian-Bo Wu Xing-Ding Zhou Dong-sheng Li Qiu-Min Lu Wan-Yu Wang Yu-Liang Xiong |
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Affiliation: | Department of Animal Toxinology, Kunming Institute of Zoology, The Chinese Academy of Sciences, Kunming 650223, China. |
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Abstract: | A hemorrhagic proteinase, jerdohagin, was purified from Trimeresurus jerdonii venom by gel filtration and ion-exchange chromatographies. It was a single chain polypeptide with an apparent molecular weight of 96 kDa as estimated by SDS-PAGE under the non-reducing and reducing conditions. Internal peptide sequencing indicated that it consisted of metalloproteinase, disintegrin-like and cysteine-rich domains and belonged to the class III snake venom metalloproteinases (class P-III SVMPs). Like other typical metalloproteinases, hemorrhagic activities of jerdohagin were completely inhibited by EDTA, but not by PMSF. Jerdohagin preferentially degraded alpha-chain of human fibrinogen. Interestingly, jerdohagin did not activate human prothrombin, whereas it cleaved human prothrombin and fragment F1 of activated human prothrombin. |
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Keywords: | Hemorrhage SVMP Trimeresurus jerdonii Fibrinogenolytic activity Activation fragment F1 |
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