CHARACTERIZATION OF CA-2+-DEPENDENT NEUTRAL PROTEASE (CALPAIN) FROM HUMAN BLOOD FLUKES, SCHISTOSOMA-MANSONI
CHARACTERIZATION OF CA-2+-DEPENDENT NEUTRAL PROTEASE (CALPAIN) FROM HUMAN BLOOD FLUKES, SCHISTOSOMA-MANSONI
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DOI：
10.1016/0925-4439(93)90087-h
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发表时间：
1993-03-24
期刊：
影响因子：
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通讯作者：
CLARKE, MW
中科院分区：
文献类型：
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作者：
SIDDIQUI, AA;ZHOU, Y;CLARKE, MW
钙依赖性中性半胱氨酸蛋白酶（钙蛋白酶）纯化人血吸虫，血吸虫曼氏。电泳迁移率，蛋白质印迹分析和肽抑制剂的高特异性证实了钙蛋白酶I和II在纯化的制剂中的存在。胞浆钙蛋白酶定位于表面的合胞上皮和下面的肌肉组织。使用肽抑制剂，钙蛋白酶被证明是作为一个调解人的表面膜合成过程。由于也没有脊椎动物和寄生虫钙蛋白酶之间的免疫交叉反应性，使用抗体亲和纯化的天然和重组寄生虫钙蛋白酶，这种蛋白酶可能是有用的研究，形成的基础上，针对血吸虫病的分子疫苗。
Calcium-dependent, neutral cysteine-proteases (calpain) were purified from human blood flukes, Schistosoma mansoni. The electrophoretic mobilities, Western blot analyses and high specificity to peptide inhibitors confirmed the presence of both calpain I and II in the purified preparation. The schistosome calpains were localized in the surface syncytial epithelium and underlying musculature. Using peptide inhibitors, calpain was shown to function as a mediator of the surface membrane synthetic process. Since there was also no immunological cross-reactivity between vertebrate and schistosome calpains using antibodies affinity-purified from native and recombinant schistosome calpains, this protease may be usefully investigated as forming the basis of a molecular vaccine against schistosomiasis.