SEPARATION BY CATION-EXCHANGE HIGH-PERFORMANCE LIQUID-CHROMATOGRAPHY OF 3 FORMS OF CHINESE HAMSTER OVARY CELL-DERIVED RECOMBINANT HUMAN INTERLEUKIN-2

被引:8
|
作者
MARCHESE, E
VITA, N
MAUREAUD, T
FERRARA, P
机构
[1] Unité Biochimie des Proteines, Sanofi Elf Bio-Recherches, 31328 Labège Cédex
来源
JOURNAL OF CHROMATOGRAPHY | 1990年 / 504卷 / 02期
关键词
D O I
10.1016/S0021-9673(01)89538-8
中图分类号
O65 [分析化学];
学科分类号
070302 ; 081704 ;
摘要
Purified recombinant (r) interleukin 2 (IL-2) produced by a transformed Chinese hamster ovary cell line shows a single peak when analysed by reversed-phase high-performance liquid chromatography, but it can be resolved into three forms by sodium dodecyl sulphate polyacrylamide gel electrophoresis. These three forms were successfully isolated by narrow-bore ion-exchange chromatography through optimization of the elution conditions. The addition of n-propanol as an organic modifier to the mobile phase proved to be essential for the recovery of the protein from the column in a yield of 90% or better based on protein quantification and biological activity determination. This chromatographic method was used for the purification of these three rIL-2 forms which represent variable glycosylation of a single polypeptide chain. A comparison of the biological activities using the murine CTLL-2 cell proliferation assay showed that the specific activities of the three forms are similar. © 1990.
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页码:351 / 358
页数:8
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