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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제18권 제10호
- 발행연도
- 2008.1
- 수록면
- 1,648 - 1,654 (7page)
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초록· 키워드
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Superoxide dismutase (SOD) removes damaging reactive oxygen species from the cellular environment by catalyzing the dismutation of two superoxide radicals to hydrogen peroxide and oxygen. Extracellular superoxide dismutase (EC-SOD) is a tetramer and is present in the extracellular space and to a lesser extent in the extracellular fluids.
Increasing therapeutic applications for recombinant human extracellular superoxide dismutase (rEC-SOD) has broadened interest in optimizing methods for its purification, with a native conformation of tetramer. We describe a solid phase refolding procedure that combines immobilized metal affinity chromatography (IMAC) and gel filtration chromatography in the purification of rEC-SOD from Escherichia coli. The purified rEC-SOD tetramer from the Ni2+-column chromatography is refolded in Tris buffer.
This method yields greater than 90% of the tetramer form. Greater than 99% purity is achieved with further purification over a Superose 12PC 3.2/30 column to obtain the tetramer and specific activities as determined via DCFHDA assay. The improved yield of rEC-SOD in a simple chromatographic purification procedure promises to enhance the development and therapeutic application of this biologically potent molecule.
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참고문헌 (21)
참고문헌 신청
Bowler, R. P. / 2002 / Furin proteolytically processes the heparin-binding region of extracellular superoxide dismutase. J. Biol / Chem 277 : 16505 ~ 16511
Bradford, M. M. / 1976 / A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal / Biochem 7
Carlsson, L. M. / 1996 / The rat extracellular superoxide dismutase dimer is converted to a tetramer by the exchange of a single amino acid. Proc. Natl / Acad. Sci 93 : 5219
Enghild, J. J. / 1999 / The heparin-binding domain of extracellular superoxide dismutase is proteolytically processed intracellularly during biosynthesis. J. Biol / Chem 274
Fattman, C. L. / 2001 / Altered expression of extracellular superoxide dismutase in mouse lung after bleomycin treatment. Free Radic / Biol. Med 31 : 1198 ~ 1207
Bradford, M. M. / 1976 / A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal / Biochem 7
Carlsson, L. M. / 1996 / The rat extracellular superoxide dismutase dimer is converted to a tetramer by the exchange of a single amino acid. Proc. Natl / Acad. Sci 93 : 5219
Enghild, J. J. / 1999 / The heparin-binding domain of extracellular superoxide dismutase is proteolytically processed intracellularly during biosynthesis. J. Biol / Chem 274
Fattman, C. L. / 2001 / Altered expression of extracellular superoxide dismutase in mouse lung after bleomycin treatment. Free Radic / Biol. Med 31 : 1198 ~ 1207
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