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首页> 外文期刊>Journal of biochemical and molecular toxicology >Hemorrhagic metalloproteinase, Cc HSM‐III, isolated from Cerastes cerastes Cerastes cerastes venom: Purification and biochemical characterization
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Hemorrhagic metalloproteinase, Cc HSM‐III, isolated from Cerastes cerastes Cerastes cerastes venom: Purification and biochemical characterization

机译:血液腐蚀金属蛋白酶,CC HSM-III,来自CERASTESSCERASTESSCERASTES毒液:纯化和生化表征

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摘要

Abstract Snake venom metalloproteinases are the most abundant toxins in Viperidae venoms. In this study, a new hemorrhagin, Cc HSM‐III (66 kDa), was purified from Cerastes cerastes venom by gel filtration, ion exchange, and reversed‐phase high‐performance liquid chromatographies. The analysis of Cc HSM‐III by liquid chromatography with a tandem mass spectrometry revealed 32 peptides sharing a homology with P‐III metalloproteinases from Echis ocellatus snake venom. Cc HSM‐III displays hemorrhagic activity with a minimal hemorrhagic dose of 5 μg, which is abolished by ethylene diamine tetracetic acid but not by phenylmethylsulfonyl fluoride. The mechanism underlying Cc HSM‐III hemorrhagic activity is probably due to its extensive proteolytic activity against type IV collagen. Cc HSM‐III induces local tissue damage and an inflammatory response by upregulating both matrix metalloproteinase 2 and 9 in skin of mice. Thus, Cc HSM‐III may play a key role in the pathogenesis of C. cerastes envenomation.
机译:摘要蛇毒液金属蛋白酶是Viperidae毒液中最丰富的毒素。在本研究中,通过凝胶过滤,离子交换和反相高效液相色谱,从激动纤维毒液中纯化新的Heorrhagin,CC HSM-III(66 kDa)。用串联质谱法分析CC HSM-III液相色谱分析显示32肽与来自Echis Ocellatus蛇毒液的P-III金属蛋白酶分享同源性的肽。 CC HSM-III显示出具有5μg的最小出血剂量的出血性活性,其被乙烯二胺四乙酸废除,而不是通过苯基甲基磺酰芳酰胺。 CC HSM-III出血活动的机制可能是由于其针对IV型胶原蛋白的广泛蛋白水解活性。 CC HSM-III通过将基质金属蛋白酶2和2和9的小鼠皮肤上调诱导局部组织损伤和炎症反应。因此,CC HSM-III可能在C.蠕动envenomation的发病机制中发挥关键作用。

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