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Structure of recombinant human carboxylesterase 1 isolated from whole cabbage looper larvae

机译:大白菜cabbage幼虫中重组人羧酸酯酶1的结构

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摘要

The use of whole insect larvae as a source of recombinant proteins offers a more cost-effective method of producing large quantities of human proteins than conventional cell-culture approaches. Human carboxylesterase 1 has been produced in and isolated from whole Trichoplusia ni larvae. The recombinant protein was crystallized and its structure was solved to 2.2 Å resolution. The results indicate that the larvae-produced enzyme is essentially identical to that isolated from cultured Sf21 cells, supporting the use of this expression system to produce recombinant enzymes for crystallization studies.
机译:与传统的细胞培养方法相比,使用整个昆虫幼虫作为重组蛋白的来源提供了一种更具成本效益的生产大量人蛋白的方法。人羧酸酯酶1已经在完整的Trichoplusia ni nivae幼虫中产生并分离出。重组蛋白结晶后,其结构解析为2.2Å分辨率。结果表明,幼虫产生的酶与从培养的Sf21细胞分离的酶基本相同,支持使用该表达系统产生用于结晶研究的重组酶。

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