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[取决于重折叠条件,肠肽酶在特定接头(天冬氨酸)4赖氨酸处对嵌合蛋白的水解作用]

[Hydrolysis of chimeric proteins by enteropeptidase at the specific linker (Asp)4Lys depending on refolding conditions].

作者信息

Shibanova E D, Mikhaĭlova A G, Aleksandrov S L, Rumsh L D

机构信息

Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.

出版信息

Bioorg Khim. 2000 Jul;26(7):522-9.

Abstract

Refolding from inclusion bodies of chimeric proteins containing the enteropeptidase-specific linker (Asp)4Lys was carried out. It was shown that, depending on the refolding conditions, chimeric proteins function as substrates or inhibitors of the enteropeptidase. The efficiency of the enteropeptidase hydrolysis of chimeric proteins containing the (Asp)4Lys linker may depend not only on the amino acid sequence of the protein binding site for the enzyme but also on the site conformation.

摘要

对含有肠肽酶特异性接头(Asp)4Lys的嵌合蛋白包涵体进行了复性。结果表明,根据复性条件,嵌合蛋白可作为肠肽酶的底物或抑制剂。含有(Asp)4Lys接头的嵌合蛋白的肠肽酶水解效率不仅可能取决于酶的蛋白结合位点的氨基酸序列,还可能取决于该位点的构象。

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