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首页> 外文期刊>Journal of biochemical and molecular toxicology >Biochemical and biological characterization of a dermonecrotic metalloproteinase isolated from Cerastes cerastes snake venom
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Biochemical and biological characterization of a dermonecrotic metalloproteinase isolated from Cerastes cerastes snake venom

机译：从斯科斯斯科斯蛇毒液中分离的DerceCecric Metallotinase的生物化学和生物学特征

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摘要

A dermonecrotic metalloproteinase (CcD-II) was isolated from C. cerastes venom. Venom fractionation was performed using three chromatographic steps (molecular exclusion on Sephadex G-75, ion-exchange on DEAE-Sephadex A-50, and reversed-phase high-performance liquid chromatography on C8 column). CcD-II presented an apparent molecular mass of 39.9 kDa and displayed a dermonecrotic activity with a minimal necrotic dose of 0.2 mg/kg body weight. CcD-II showed proteolytic ability on casein chains and on alpha and beta fibrinogen chains that was inhibited by ethylenediamine tetraacetic acid and 1,10-phenanthroline while remained unaffected by phenylmethylsulphonyl fluoride and heparin. CcD-II displayed gelatinase activity and degraded extracellular matrix compounds (type-IV collagen and laminin). These results correlated with histopathological analysis showing a complete disorganization of collagenous skin fibers. These data suggested that CcD-II belongs to P-II class of snake venom metalloproteinase. The characterization of venom compounds involved in tissue damage may contribute in the development of new therapeutic strategies in envenomation.
机译：从C.Cerastes毒液中分离出一种DercoCecric Metallotinase（CCD-II）。使用三个色谱步骤（Sephadex G-75上的分子排阻，在DEAE-Sephadex A-50上的离子交换，以及C8塔上的反相高效液相色谱法进行毒液分馏。 CCD-II呈现出39.9kDa的表观分子量，并显示出具有0.2mg / kg体重的最小黑分子剂量的DercoSecrist活性。 CCD-II显示酪蛋白链和α和β纤维蛋白原链的蛋白水解能力，其被乙二胺四乙酸和1,10菲咯啉抑制的，同时依赖于苯基甲基磺酰基和肝素的影响。 CCD-II显示凝胶酶活性和降解细胞外基质化合物（IV型胶原蛋白和层粘连蛋白）。这些结果与显示胶原皮肤纤维的完全紊乱的组织病理学分析相关。这些数据表明CCD-II属于P-II类蛇毒液金属蛋白酶。涉及组织损伤的毒液化合物的表征可能有助于在envenomation中的新治疗策略的发展中有助于。

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