Hale R S, Thompson G
Biomolecular Structure Unit, GlaxoWellcome R & D, Stevenage, United Kingdom.
Protein Expr Purif. 1998 Mar;12(2):185-8. doi: 10.1006/prep.1997.0825.
An internal domain from the human type 1 neurofibromin has previously been expressed in Escherichia coli as a fusion with gluthathione S-transferase (GST). The expression level of this protein was lower than expected and so a gene was constructed using the distribution of codons found in highly expressed E. coli proteins. Codons were assigned using a Microsoft Visual Basic computer program to give a distribution similar to those found in genes which are highly expressed in E. coli. The optimized gene was then cloned back into the same GST fusion plasmid and it was found that the expression of soluble protein had increased threefold.
人类1型神经纤维瘤蛋白的一个内部结构域先前已在大肠杆菌中作为与谷胱甘肽S-转移酶（GST）的融合蛋白表达。该蛋白的表达水平低于预期，因此利用在高表达的大肠杆菌蛋白中发现的密码子分布构建了一个基因。使用微软Visual Basic计算机程序分配密码子，使其分布与在大肠杆菌中高表达的基因中发现的分布相似。然后将优化后的基因克隆回同一GST融合质粒中，发现可溶性蛋白的表达增加了三倍。
