Purification and characterization of recombinant human interleukin 5 expressed in Chinese hamster ovary cells

Journal of Biochemistry
M TsujimotoK Takatsu

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.

Citations

Jan 1, 1991·Microbiology and Immunology·K Takatsu
Mar 1, 1991·Clinical and Experimental Immunology·K TomizawaS Matsumoto
Jun 13, 1997·The Journal of Biological Chemistry·M TsujimotoN Yamaguchi
Feb 1, 1993·European Journal of Biochemistry·S KodamaA Kobata
Apr 1, 1991·Cellular Immunology·M MigitaK Takatsu
Feb 1, 1992·Archives of Biochemistry and Biophysics·B B Aggarwal, E Pocsik
Jul 31, 1991·Biochemical and Biophysical Research Communications·S KodamaM Tsujimoto

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