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Isolation of intramembrane proteases in membrane-like environments.
Biochimica et Biophysica Acta (BBA) - Biomembranes ( IF 3.4 ) Pub Date : 2020-01-13 , DOI: 10.1016/j.bbamem.2020.183193
Marta Barniol-Xicota 1 , Steven H L Verhelst 2
Affiliation  

Intramembrane proteases (IMPs) are proteolytic enzymes embedded in the lipid bilayer, where they cleave transmembrane substrates. The importance of IMPs relies on their role in a wide variety of cellular processes and diseases. In order to study the activity and function of IMPs, their purified form is often desired. The production of pure and active IMPs has proven to be a challenging task. This process unavoidably requires the use of solubilizing agents that will, to some extent, alter the native environment of these proteases. In this review we present the current solubilization and reconstitution techniques that have been applied to IMPs. In addition, we describe how these techniques had an influence on the activity and structural studies of IMPs, focusing on rhomboid proteases and γ-secretase.

中文翻译:

在膜样环境中分离膜内蛋白酶。

膜内蛋白酶(IMPs)是包埋在脂质双层中的蛋白水解酶,在脂质双层中它们裂解跨膜底物。IMP的重要性取决于它们在多种细胞过程和疾病中的作用。为了研究IMP的活性和功能,经常需要它们的纯化形式。事实证明,生产纯净的和活性的IMPs是一项艰巨的任务。该过程不可避免地需要使用增溶剂,这将在一定程度上改变这些蛋白酶的天然环境。在这篇综述中,我们介绍了目前应用于IMP的增溶和重构技术。另外,我们描述了这些技术如何影响IMP的活性和结构研究,重点是菱形蛋白酶和γ-分泌酶。
更新日期:2020-01-13
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