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

被引：8

作者：

GUISEZ, Y ^{[1
]}

OEFNER, C ^{[1
]}

WINKLER, FK ^{[1
]}

SCHLAEGER, EJ ^{[1
]}

ZULAUF, M ^{[1
]}

VANDERHEYDEN, J ^{[1
]}

PLAETINCK, G ^{[1
]}

CORNELIS, S ^{[1
]}

TAVERNIER, J ^{[1
]}

FIERS, W ^{[1
]}

DEVOS, R ^{[1
]}

DARCY, A ^{[1
]}

机构：

[1] F HOFFMANN LA ROCHE & CO LTD,DEPT PHARMACEUT RES,CH-4002 BASEL,SWITZERLAND

来源：

FEBS LETTERS | 1993年 / 331卷 / 1-2期

关键词：

LARGE SCALE PRODUCTION; RECOMBINANT HIL-5; SF9 INSECT CELL; BACULOVIRUS; IMMUNOAFFINITY CHROMATOGRAPHY; PRELIMINARY CRYSTALLOGRAPHIC ANALYSIS;

D O I：

10.1016/0014-5793(93)80295-6

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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 angstrom.

引用

页码：49 / 52

页数：4

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