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首页> 外文期刊>The Journal of toxicological sciences >Purification and characterization of five snake venom metalloproteinases from egyptian echis pyramidum pyramidum venom
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Purification and characterization of five snake venom metalloproteinases from egyptian echis pyramidum pyramidum venom

机译：埃及蛇皮金字塔状蛇毒中五种蛇毒金属蛋白酶的纯化和鉴定

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摘要

New five P-III snake venom metalloproteinases (SVMPs): EpyB2 (62 kDa), EpyB3 (62+23 kDa), EpyB4 (60 kDa), EpyB5 (67 kDa) and EpyB6 (66 kDa) of the most dangerous viper, Echis pyramidum pyramidum (Epy), were purified and characterized in a set of biochemical assays. The SVMPs were purified by applying a protocol of two successive chromatographic steps. Three purified SVMPs "EpyB2, EpyB4, and EpyB5" have hemorrhagic activity with MHDs, 7 μg, 7.6 μg and 15 μg, respectively; furthermore, they have high preference towards fibronectin, collagen, gelatin, fibrin and hemoglobin substrates compared with non-hemorrhagic SVMPs (EpyB3 and EpyB6). All the purified SVMPs showed remarkable thermal and pH stability, inhibited by metalloproteinase inhibitors and Zn2+, Mn2+, Ni2+, Co2+, Cu2+, and Hg2+. The purified SVMPs act as α-fibrinogenases, prothrombin activators and procoagulants. In conclusion, Epy venom has multiple SVMPs that are responsible for hemorrhagic events and thus represent a significant health hazard for victims of envenomation, however, they may be useful for treating diseases involving abnormal blood clot formation.
机译：新的五种P-III蛇毒金属蛋白酶（SVMP）：最危险的毒蛇EchiB2（62 kDa），EpyB3（62 + 23 kDa），EpyB4（60 kDa），EpyB5（67 kDa）和EpyB6（66 kDa）金字塔金字塔（Epy），已通过一系列生化分析进行了纯化和表征。通过应用两个连续色谱步骤的方案纯化SVMP。三种纯化的SVMP“ EpyB2，EpyB4和EpyB5”具有MHD的出血活性，分别为7μg，7.6μg和15μg;此外，与非出血性SVMP（EpyB3和EpyB6）相比，它们对纤连蛋白，胶原蛋白，明胶，纤维蛋白和血红蛋白底物具有更高的偏好。所有纯化的SVMP均表现出卓越的热稳定性和pH稳定性，并受到金属蛋白酶抑制剂和Zn2 +，Mn2 +，Ni2 +，Co2 +，Cu2 +和Hg2 +的抑制。纯化的SVMP充当α-纤维蛋白原酶，凝血酶原激活剂和促凝剂。总之，Epy毒液具有多种导致出血事件的SVMP，因此对被毒化的受害者构成重大健康危害，但是，它们可用于治疗涉及异常血块形成的疾病。

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