EXPRESSION, PURIFICATION AND CRYSTALLIZATION OF FULLY ACTIVE, GLYCOSYLATED HUMAN INTERLEUKIN-5

Authors
GUISEZ Y OEFNER C WINKLER FK SCHLAEGER EJ ZULAUF M VANDERHEYDEN J PLAETINCK G CORNELIS S TAVERNIER J FIERS W DEVOS R DARCY A
Citation
Y. Guisez et al., EXPRESSION, PURIFICATION AND CRYSTALLIZATION OF FULLY ACTIVE, GLYCOSYLATED HUMAN INTERLEUKIN-5, FEBS letters, 331(1-2), 1993, pp. 49-52
Citations number
35
Categorie Soggetti
Biophysics,Biology
Journal title
FEBS letters → ACNP
ISSN journal
00145793
Volume
331
Issue
1-2
Year of publication
1993
Pages
49 - 52
Database
ISI
SICI code
0014-5793(1993)331:1-2<49:EPACOF>2.0.ZU;2-Z
Abstract
Recombinant human interleukin-5 (hIL-5) has been expressed at high lev els and produced in large quantities in baculovirus infected Sf9 insec t cells. The glycosylated protein was purified using immuno-affinity c hromatography and gel filtration. Purified hIL-5 has been crystallized using standard vapour diffusion techniques with PEG as a coprecipitan t. The crystals belong to the C2 space group and diffract to 2 angstro m.