Recombinant human interleukin-2 : I. purification and biochemical characterization

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Recombinant human interleukin-2 : I. purification and biochemical characterization
Hye-Young Yun; Hye-Lim Choi; Myung Kyu Lee; Seung Ho Kim; Doe Sun Na; Sun Bok Lee; Moon Hi Han; Kyung Soo Hahm
Bibliographic Citation
Korean Biochemical Journal, vol. 21, no. 2, pp. 120-126
Publication Year
Recombinant human interleukin-2 (rH IL-2, Ser125-rH IL-2) was purified to apparent homogeneity from E. coli in high yield and characterized its biochemical properties for the establishment of preclinical screening system and therapeutic applications. The purification was carried out by methods involving isolation of inclusion body, urea extraction, solubilization and gel filtration chromatography. The renaturation of the product was achieved by extensive dialysis against the storage buffer. The purity was confirmed by SDS-PAGE and HPLC. Amino terminal amino acid analysis and partial amino acid sequence analysis showed that the primary structure of the recombinant protein (rH IL-2) was found to be identical with natural IL-2. The purity and the conformation of the rH IL-2 were also confirmed by obtaining crystals of the recombinant nrotein.
Korea Soc-Assoc-Inst
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1. Journal Articles > Journal Articles
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