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Expression, purification and crystallization of fully active, glycosylated human interleukin‐5
Author(s) -
Guisez Yves,
Oefner Christian,
Winkler Fritz K.,
Schlaeger Ernst-Jürgen,
Zulauf Martin,
Van der Heyden José,
Plaetinck Geert,
Cornells Sigrid,
Tavernier Jan,
Fiers Walter,
Devos René,
D'Arcy Allan
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80295-6
Subject(s) - sf9 , recombinant dna , size exclusion chromatography , affinity chromatography , crystallization , chemistry , chromatography , peg ratio , glycoprotein , glycosylation , monoclonal antibody , biochemistry , biology , antibody , spodoptera , immunology , organic chemistry , enzyme , finance , economics , gene
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.