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背景:小分子热休克蛋白Hsp16.3具有分子伴侣活性,在体外对其它蛋白质的正确折叠可能具有一定的作用。结核分枝杆菌38kD蛋白(简称38kD蛋白)在大肠杆菌中表达后主要以包涵体的形式存在,本实验室有人曾研究将Hsp16.3与38kD蛋白分别克隆到不同的质粒在同一宿主菌中共表达后,发现38kD蛋白仍然以包涵体的形式存在。本研究是将Hsp16.3基因和38kD基因融合,观察融合基因的表达情况。 目的:探讨Hsp16.3基因在融合后,对融合
Background: The small molecule heat shock protein Hsp16.3 has chaperone activity and may play a role in the correct folding of other proteins in vitro. Mycobacterium tuberculosis 38kD protein (referred to as 38kD protein) expressed in E. coli mainly in the form of inclusion bodies, some people in our laboratory have been studied Hsp16.3 and 38kD proteins were cloned into different plasmids in the same host co-expression After that, the 38 kD protein was found to still exist as an inclusion body. In this study, Hsp16.3 gene and 38kD gene were fused to observe the expression of the fusion gene. Objective: To investigate the fusion of Hsp16.3 gene after fusion