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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Subunit cleavage of mosquito pro-vitellogenin by a subtilisin-like convertase
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Subunit cleavage of mosquito pro-vitellogenin by a subtilisin-like convertase

机译:枯草杆菌蛋白酶样转化酶裂解蚊原玻璃素原的亚基

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摘要

The eukaryotic convertase family plays an important role in posttranslational proteolytic processing and activation of many pro- and polypeptides that have at their cleavage sites the paired basic motif, RX(K/R)R. Recent studies have revealed that the cleavage site of insect pro- vitellogenins (pro-Vg) also contains this motif. To identify and characterize the insect pro-Vg processing enzyme, Vg conver- tase (VC), its cDNA was cloned from a vitellogenic female fat body cDNA library of the mosquito, Aedes aegypti.
机译:真核转化酶家族在翻译后蛋白水解过程和许多在其切割位点具有配对基本基序RX(K / R)R的原蛋白和多肽的活化中起着重要作用。最近的研究表明,昆虫卵黄蛋白原(pro-Vg)的切割位点也含有该基序。为了鉴定和表征昆虫前Vg加工酶Vg转化酶(VC),从蚊子埃及伊蚊的产卵母性雌性脂肪cDNA文库中克隆了其cDNA。

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