Production, Purification and Immuno-Modulatory Actions of E. coli-derived Recombinant Human Interleukin 4대장균에서 재조합 인간 interleukin 4의 생산, 정제 및 면역조절활성의 측정
- Other Titles
- 대장균에서 재조합 인간 interleukin 4의 생산, 정제 및 면역조절활성의 측정
- Authors
- 양영; 윤석란; 이충은; 변광호
- Issue Date
- Jan-1992
- Publisher
- Korea Soc-Assoc-Inst (생화학분자생물학회)
- Citation
- Korean Biochemical Journal, v.25, no.1, pp 66 - 72
- Pages
- 7
- Journal Title
- Korean Biochemical Journal
- Volume
- 25
- Number
- 1
- Start Page
- 66
- End Page
- 72
- URI
- https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/151141
- ISSN
- 1976-6696
1976-670X
- Abstract
- The recombinant human interleukin 4 (rhIL-4) has been over expressed in E. coli transformed with expression vector pET-3b containing bacteriophage T7 promoter, into which the hIL-4 cDNA was subclond. The insolubility of the recombinant protein offered an advantage of purification in only a few steps. The recombinant human IL-4 was refolded using reduced/oxidized glutathione to restore the proper conformation and purified to homogeneity by one passage over ion exchange column. The purified protein was shown as a single band on SDS-PAGE. The refolded rhIL-4 was characterized by nucleotide sequence analysis and bioassays. The purified rhIL-4 has biological activities on B cell proliferation and induction of B cell differentiation antigen, CD23, which strongly indicates that the protein is folded correctly.
- Files in This Item
-
Go to Link
- Appears in
Collections - 이과대학 > 생명시스템학부 > 1. Journal Articles
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.