猪笼草蛋白酶在尿素和盐酸胍中的稳定性研究：与猪胃蛋白酶A的比较。
Stability profiles of nepenthesin in urea and guanidine hydrochloride: comparison with porcine pepsin A.
作者信息
Kubota Keiko, Metoki Yuya, Athauda Senarath B P, Shibata Chiaki, Takahashi Kenji
机构信息
Laboratory of Molecular Biochemistry, School of Life Sciences, Tokyo University of Pharmacy and Life Sciences, Hachioji, Japan.
出版信息
Biosci Biotechnol Biochem. 2010;74(11):2323-6. doi: 10.1271/bbb.100391. Epub 2010 Nov 7.
Nepenthesin, an aspartic endopeptidase from the pitcher fluid of Nepenthes, was found to be markedly less stable than porcine pepsin A when treated with urea or guanidine hydrochloride. This is in sharp contrast with its remarkably high pH/temperature stability as compared with porcine pepsin A. No protein with such a stability profile has been reported to date.
猪笼草蛋白酶是一种来自猪笼草捕虫笼液体的天冬氨酸内肽酶，研究发现，在用尿素或盐酸胍处理时，它的稳定性明显低于猪胃蛋白酶A。这与它和猪胃蛋白酶A相比具有显著的高pH/温度稳定性形成了鲜明对比。迄今为止，尚未报道过具有这种稳定性特征的蛋白质。
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