한국미생물·생명공학회지 (Microbiology and Biotechnology Letters)
- 제13권1호
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- Pages.87-91
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- 1985
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- 1598-642X(pISSN)
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- 2234-7305(eISSN)
Hpa I endonuclease의 정제와 특성
Purification and Characterization of Hpa I endonuclease
- Yoon, Ho Sup (Department of Biological Science and Engineering, Korea Advanced Institute of Science and Technology) ;
- Kang, Sun Chul (Department of Biological Science and Engineering, Korea Advanced Institute of Science and Technology) ;
- Yoo, Ouk Joon (Department of Biological Science and Engineering, Korea Advanced Institute of Science and Technology)
- 투고 : 1985.03.06
- 발행 : 1985.03.01
초록
Hpa I endonuclease를 순수 정제하였다. 150g (wet weight)의 Haemophilus parainfluenzae로 부터 얻은 crude extract를 ammonium sulfate fractionation을 거친후 Heparin agarose, SP-sephadex, DEAE-sephadex, phosphocellulose 등 chromatography를 거쳐 최종적으로 0.2mg의 효소를 얻었다. Specific activity는
Hpa I endonuclease from Haemophilus parainfluenzae has been purified of homogeneity and its physical and ezymatic properties have been studied. For the purification of the enzyme, Heparin agarose, SP-sephadex C-25, DEAE-sephadex A-50 and phosphocellulose chromatography columns were used. The denatured and reduced form of the enzyme is a monomer of molecular weight of
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