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来自巴西利什曼原虫的铁超氧化物歧化酶的分子克隆与生化特性分析

Molecular Cloning and Biochemical Characterization of Iron Superoxide Dismutase from Leishmania braziliensis.

作者信息

Brito Camila C B, Maluf Fernando V, de Lima Gustavo M A, Guido Rafael V C, Castilho Marcelo S

机构信息

Programa de pós-graduação em Biotecnologia, Universidade Estadual de Feira de Santana, Feira de Santana, BA, Brazil.

Sao Carlos Institute of Physics, University of Sao Paulo, Av. Joao Dagnone, 1100 Jardim Santa Angelina, São Carlos, SP, 13563-120, Brazil.

出版信息

Mol Biotechnol. 2018 Aug;60(8):595-600. doi: 10.1007/s12033-018-0095-2.

DOI:10.1007/s12033-018-0095-2
PMID:29951736
Abstract

Leishmaniasis is one of the most important neglected tropical diseases, with a broad spectrum of clinical manifestations. Among the clinical manifestations of the disease, cutaneous leishmaniasis, caused by species of Leishmania braziliensis, presents wide distribution in Brazil. In this work, we performed the cloning, expression, and purification of the enzyme superoxide dismutase of Leishmania braziliensis (LbSOD-B2) considered a promising target for the search of new compounds against leishmaniasis. In vitro assays based on pyrogallol oxidation showed that LbSOD-B2 is most active around pH 8 and hydrogen peroxide is a LbSOD-B2 inhibitor at low millimolar range (IC = 1 mM).

摘要

利什曼病是最重要的被忽视的热带病之一,具有广泛的临床表现。在该疾病的临床表现中,由巴西利什曼原虫引起的皮肤利什曼病在巴西广泛分布。在这项工作中,我们对巴西利什曼原虫的超氧化物歧化酶(LbSOD-B2)进行了克隆、表达和纯化,该酶被认为是寻找抗利什曼病新化合物的一个有前景的靶点。基于邻苯三酚氧化的体外试验表明,LbSOD-B2在pH 8左右活性最高,过氧化氢在低毫摩尔范围内是LbSOD-B2的抑制剂(IC = 1 mM)。

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