Expression, purification and crystallization of fully active, glycosylated human interleukin‐5

FEBS Letters

Devos, René¹  Fiers, Walter¹  Plaetinck, Geert¹  Guisez, Yves¹  Winkler, Fritz K.²  Oefner, Christian²  Zulauf, Martin²  Cornells, Sigrid¹  Van der Heyden, José¹  Schlaeger, Ernst-Jürgen²  D'Arcy, Allan²  Tavernier, Jan¹ 

[1] Roche Research Gent, Jozef Plateaustraat 22, B-9000 Gent, Belgium;Department of Pharmaceutical Research, New Technologies F. Hoffmann-La Roche Ltd., Basel, Switzerland

关键词: Large scale production;    Recombinant hIL-5;    Sf9 insect cell;    Baculovirus;    Immuno-affinity chromatography;    Preliminary crystallographic analysis;   

DOI  :  10.1016/0014-5793(93)80295-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Recombinant human interleukin-5 (hIL-5) has been expressed at high levels and produced in large quantities in baculovirus infected Sf9 insect cells. The glycosylated protein was purified using immuno-affinity chromatography and gel filtration. Purified hIL-5 has been crystallized using standard vapour diffusion techniques with PEG as a coprecipitant. The crystals belong to the C2 space group and diffract to 2 Å.

【 授权许可】

Unknown