短通信:C57BL/6小鼠对照蛋白cDNA的克隆与序列分析

Koji Yoshida, Yasuyuki Suzuki, H. Sinohara
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引用次数: 2

摘要

Contrapsin是serpin超家族的一员,对胰蛋白酶的抑制作用比αi-抗蛋白酶强得多。小鼠和大鼠对照蛋白序列与人α1 -抗凝乳胰蛋白酶相似。为了验证contrapsin家族活性位点区域是在强选择压力下进化的假设,我们测定了C57BL/6小鼠contrapsin的cDNA序列,并与ICR小鼠进行了比较。C57BL/6小鼠对照蛋白cDNA序列包含一个开放阅读框,编码由418个氨基酸残基组成的多肽。本文的工作表明,与分子的其他部分相比,反应位点并不高变。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Short Communication: Molecular Cloning and Sequence Analysis of C57BL/6 Mouse Contrapsin cDNA
Contrapsin is a member of the serpin superfamily and inhibits trypsin much more strongly than αi-antiproteinase. Mouse and rat contrapsins, however, have similarity in sequence to human α1 -antichymotrypsin. In order to test the hypothesis that reactive site regions of contrapsin family evolved under strong selective pressure, cDNA sequence of C57BL/6 mouse contrapsin was determined and compared with that of ICR mouse. The cDNA sequence of C57BL/6 mouse contrapsin was found to contain an open reading frame encoding polypeptide consisting of 418 amino acid residues. The work reported in this paper shows that the reactive site is not hypervariable as compared with the rest of molecule.
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