재조합 인체 인터루킨 - 2 1 . 분리정제 및 생화학적 특성

Recombinant human interleukin-2 (rH IL-2, Ser^(125)-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 in...

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Published inBMB reports Vol. 21; no. 2; pp. 120 - 126
Main Authors 윤혜영, 최혜림, 이명규, 김승호, 나도선, 이선복, 한문희, 함경수, Hye - Young Yun, Hye - Lim Choi, Myeong Kyu Lee, Seung Ho Kim, Doe Sun Na, Sun Bok Lee, Moon H . Han, Kyung - Soo Hahm
Format Journal Article
LanguageKorean
Published 생화학분자생물학회 01.01.1988
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Summary:Recombinant human interleukin-2 (rH IL-2, Ser^(125)-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 protein.
Bibliography:Korean Society for Biochemistry and Molecular Biology
ISSN:1976-6696