GLUTATHIONE TRANSFERASES IN THE TAPEWORM MONIEZIA-EXPANSA
GLUTATHIONE TRANSFERASES IN THE TAPEWORM MONIEZIA-EXPANSA
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DOI：
10.1042/bj2620939
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发表时间：
1989-09-15
影响因子：
4.1
通讯作者：
BARRETT, J
中科院分区：
文献类型：
--
作者：
BROPHY, PM;SOUTHAN, C;BARRETT, J
通过 GSH-Sepharose 亲和层析和 pH 6-4 范围内的色谱聚焦，从 Moniezia expansa 胞质中分离出了四种形式的 GSH 转移酶，并且通过分析等电聚焦进一步表明同工酶的存在。绦虫中的四种谷胱甘肽转移酶形式与任何一种哺乳动物谷胱甘肽转移酶家族都没有明显的生化关系。主要 GSH 转移酶形式的 N 端显示出与 mu 和 Alpha 家族 GSH 转移酶的序列同源性。主要的谷胱甘肽转移酶似乎可以结合许多市售的驱虫药，但似乎不会将这些化合物与谷胱甘肽结合。主要的谷胱甘肽转移酶有效地结合反式-烷-2-烯醛和反式，反式-烷-2,4-二烯醛系列的成员，建立脂质过氧化的次级产物。
Four forms of GSH transferase were resolved from Moniezia expansa cytosol by GSH-Sepharose affinity chromatography and chromatofocusing in the range pH 6-4, and the presence of isoenzymes was further suggested by analytical isoelectric focusing. The four GSH transferase forms in the cestode showed no clear biochemical relationship to any one mammalian GSH transferase family. The N-terminal of the major GSH transferase form showed sequence homology with the mu and Alpha family GSH transferases. The major GSH transferase appeared to bind a number of commercially available anthelmintics but did not appear to conjugate the compounds with GSH. The major GSH transferase efficiently conjugated members of the trans-alk-2-enal and trans,trans-alka-2,4-dienal series, established secondary products of lipid peroxidation.