Cuervo Patrícia, Mesquita-Rodrigues Camila, d'Avila Levy Claudia Masini, Britto Constança, Pires Fabiano Araújo, Gredilha Rodrigo, Alves Carlos Roberto, Jesus Jose Batista de
Laboratório de Pesquisas em Leishmanioses, Instituto Oswaldo Cruz, Fiocruz, Rio de Janeiro, Brasil.
Mem Inst Oswaldo Cruz. 2008 Aug;103(5):504-6. doi: 10.1590/s0074-02762008000500018.
We report for the first time the expression of multiple protease activities in the first instar larva (L1) of the flesh fly Oxysarcodexia thornax (Walker). Zymographic analysis of homogenates from freshly obtained L1 revealed a complex proteolytic profile ranging from 21.5 to 136 kDa. Although some activities were detected at pH 3.5 and 5.5, the optimum pH for most of the proteolytic activities was between pH 7.5 and 9.5. Seven of 10 proteases were completely inactivated by phenyl-methyl sulfonyl-fluoride, suggesting that main proteases expressed by L1 belong to serine proteases class. Complete inactivation of all enzymatic activities was obtained using N-p-Tosyl-L-phenylalanine chloromethyl ketone (100 microM), a specific inhibitor of chymotrypsin-like serine proteases.
我们首次报道了麻蝇Oxysarcodexia thornax（Walker）一龄幼虫（L1）中多种蛋白酶活性的表达。对新鲜获取的L1匀浆进行的酶谱分析显示出一个复杂的蛋白水解图谱，范围从21.5 kDa至136 kDa。尽管在pH 3.5和5.5时检测到了一些活性，但大多数蛋白水解活性的最适pH在pH 7.5至9.5之间。10种蛋白酶中有7种被苯甲基磺酰氟完全灭活，这表明L1表达的主要蛋白酶属于丝氨酸蛋白酶类。使用N-对甲苯磺酰-L-苯丙氨酸氯甲基酮（100 microM）可完全灭活所有酶活性，它是类胰凝乳蛋白酶丝氨酸蛋白酶的特异性抑制剂。
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