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  • Title: Purification and characterization of recombinant human interleukin 5 expressed in Chinese hamster ovary cells.
    Author: Tsujimoto M, Adachi H, Kodama S, Tsuruoka N, Yamada Y, Tanaka S, Mita S, Takatsu K.
    Journal: J Biochem; 1989 Jul; 106(1):23-8. PubMed ID: 2506168.
    Abstract:
    Recombinant human interleukin 5 (rhIL-5) expressed in Chinese hamster ovary cells was purified and characterized. Molecular heterogeneity was observed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Two major components of Mr around 40,000 were detected under non-reducing conditions. However, under reducing conditions, the Mr of rhIL-5 was determined to be 22,000 and 20,000. After treatment with endoglycosidase F, a band with an apparent Mr of 18,000 was observed. Treatment of rhIL-5 with 2-mercaptoethanol followed by N-ethylmaleimide resulted in its dissociation into a monomeric form. This alkylated rhIL-5 was biologically less active than intact rhIL-5. These results suggest that rhIL-5 exists as a dimer, and that the heterogeneity of rhIL-5 is mainly due to the difference in the content of carbohydrate. Moreover, the formation of disulfide bond(s) might be important for the biological activity of rhIL-5.
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