Korean Journal of Microbiology (미생물학회지)
- Volume 23 Issue 1
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- Pages.13-19
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- 1985
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- 0440-2413(pISSN)
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- 2383-9902(eISSN)
Purification and Characterization of Acc I Endonuclease
Acc I endonuclease의 정제와 효소적 특성에 관한 연구
Abstract
Acc I endonuclease has been isolated from 300g (wet weight) cells of Acinetobacter calcoaceticus. The cells were broken by using French press at 20, 000p.s.i. After ammonium sulfate fractionation, the enzyme was further purified by heparin agarose, DEAE-sephades, Affi.-gel Blue, phosphocellulose, and hydroxylapatite column chromatography. The purified Acc I endonudlease has a single polypeptide species and its subunit molecular weight was 45,000
제한효소 Acc I을 정제하고 그 효소적 특성을 연구하였다. 300g(wet weight)의 Acinetobacter calcoaceticus 로부터 얻은 crude extract를 sample로 하여 ammonium sulfate fractionation을 거쳐 Heparin-agarose, DEAE-se-phades, Affi,-gel Blue, phosphoceIIulose, hydroxylapatite의 순서로 chromatography를 수행한 결고 0 .28mg의 AccI 제한효소를 얻었다. 효소의 specific activity는 mg당
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