胃肠道线虫和哺乳动物肝脏中谷胱甘肽s转移酶的比较

Peter M. Brophy , Anne Ben-Smith , Alan Brown , Jerzy M. Behnke , David I. Pritchard
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引用次数: 21

摘要

谷胱甘肽s -转移酶已从胃肠道线虫中部分表征。两个主要亚基家族(24和23 kDa)与哺乳动物α家族具有n端同源性。通过谷胱甘肽亲和层析、两个主要酶(pI 8.1, 5.0)和两个次要酶(pI 5.8, 5.3),从线虫中纯化了四种二聚体形式的GST。纯化后的GST池可以通过过氧化物酶活性中和模型和脂质过氧化物,但不能通过谷胱甘肽转移酶活性中和过氧化产物活性羰基。在Western blotting上,与哺乳动物GSTs相比,混合线虫GSTs的抗血清对其他Strongylida GSTs的识别能力更强。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Glutathione S-transferases from the gastrointestinal nematode Heligmosomoides polygyrus and mammalian liver compared

Glutathione S-transferases have been partially characterised from the gastrointestinal nematode Heligmosomoides polygyrus. Two major subunit families were purified (24 and 23 kDa) with N-terminal homology to the mammalian Alpha family. Four dimeric forms of GST were purified from the nematode by glutathione-affinity chromatography, two major enzymes (pI 8.1, 5.0) and two minor forms (pI 5.8, 5.3). The purified GST pool could neutralize model and lipid peroxides via peroxidase activity but not peroxidation derived reactive carbonyls via glutathione transferase activity. Antisera raised to the pooled nematode GSTs appeared to recognize other Strongylida GSTs more strongly on Western blotting compared to mammalian GSTs.

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