Ledent P, Duez C, Vanhove M, Lejeune A, Fonzé E, Charlier P, Rhazi-Filali F, Thamm I, Guillaume G, Samyn B, Devreese B, Van Beeumen J, Lamotte-Brasseur J, Frère J M
Centre for Protein Engineering, Université de Liège, Institut de Chimie, Belgium.
FEBS Lett. 1997 Aug 18;413(2):194-6. doi: 10.1016/s0014-5793(97)00908-3.
The addition of a poly-His C-terminal extension, designed to facilitate the purification of the protein, to the beta-lactamase of a thermophilic Bacillus licheniformis strain modified the site of action of the signal peptidase. This resulted in the secretion of a protein with a different N-terminus, showing that this type of protein engineering might not always be as 'neutral' as generally assumed.
在嗜热地衣芽孢杆菌菌株的β-内酰胺酶上添加一个旨在促进蛋白质纯化的多组氨酸C末端延伸，改变了信号肽酶的作用位点。这导致分泌出一种具有不同N末端的蛋白质，表明这种类型的蛋白质工程可能并不总是像通常所认为的那样“中性”。
