Expression and assembly of active human cardiac troponin in Escherichia coli

被引：3

作者：

Lassalle, Michael W. ^{[1
]}

机构：

[1] Ehime Univ, Matsuyama, Ehime 7908577, Japan

来源：

PROTEIN EXPRESSION AND PURIFICATION | 2013年 / 87卷 / 02期

关键词：

Cardiomyopathy; Human cardiac troponin; Allosteric coupling; Quartz crystal microbalance; Circular dichroism; CALCIUM-BINDING; TROPOMYOSIN; MUTATIONS; PROTEIN; COMPLEX; DOMAIN;

D O I：

10.1016/j.pep.2012.10.005

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Cardiomyopathy-related mutations in human cardiac troponin subunits, including troponin C (hcTnC), troponin I (hcTnI), and troponin T (hcTnT), are well-documented. Recently, it has been recognised that human cardiac troponin (hcTn) is a sophisticated allosteric system. Therefore, the effect of drugs on this protein complex should be studied with assembled hcTn rather than a short fragment of a subunit or the subunit itself. Here, we describe the expression and assembly of active hcTn in Escherichia coli, a novel method that is rapid and simple, and produces large amounts of functional hcTn. (C) 2012 Elsevier Inc. All rights reserved.

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页码：61 / 66

页数：6

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