Unexpected influence of a C‐terminal‐fused His‐tag on the processing of an enzyme and on the kinetic and folding parameters

FEBS Letters

Thamm, Iris²  Vanhove, Marc²  Devreese, Bart¹  Ledent, Philippe²  Lejeune, Annabelle²  Duez, Colette²  Fonzé, Eveline²  Charlier, Paulette²  Van Beeumen, Jozef¹  Lamotte-Brasseur, Josette²  Guillaume, Gilliane²  Samyn, Bart¹  Frère, Jean-Marie²  Rhazi-Filali, Fouzia³ 

[1] Vakgroep Biochemie, Fysiologie en Microbiologie, Laboratorium voor Eiwitbiochemie and Eiwitengineering Universiteit Gent, Ledeganckstraat 35, B-9000 Ghent Belgium;Centre for Protein Engineering, Université de Liège, Institut de Chimie (B6), Sart-Tilman, B-4000 Liège, Belgium;Faculté des Sciences, Université de Meknes, PO Box 4010, Meknes, Morocco

关键词: His-tag;    β-Lactamase;    Bacillus;    Thermophile;   

DOI  :  10.1016/S0014-5793(97)00908-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The addition of a poly-His C-terminal extension, designed to facilitate the purification of the protein, to the β-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.

【 授权许可】

Unknown