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RISS 인기검색어
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- 저자 : 유욱준 ( Sun Chul Kang (검색결과 4 건)
- 무료
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강선철,윤호섭,유욱준,Kang, Sun-Chul,Yoon, Ho-Sup,Yoo, O. Joon 생화학분자생물학회 1986 한국생화학회지 Vol.19 No.1
Alu I methylase로 변형시킨 DNA는 Alu I 특정 염기 배열을 내부에 공통적으로 가지고 있는 제한효소들 즉, Hind III, Sst I, Pvu II, Sac I들에 의하여 정상적으로 절단되지 않았다. 이 효소들의 반응 결과를 정량적으로 분석하기 위하여 tritium으로 label된 pBR 322 DNA와 pPG 3282 DNA를 사용하였는데 pBR 322 DNA에는 Hind III와 Pvu II site가 각각 1 개씩, pPG 3282 DNA에는 Sst I과 Sac I site가 각각 1개씩 있는 점이 절단된 후의 분석하기에 용이하기 때문이다. 각각의 경우를 분석한 결과로부터 다음과 같은 결론을 얻을 수 있었다 : (1) Sst I endonuclease가 Alu I methylase에 의해 methylation된 DNA를 느리게라도 절단할 수 있는 점으로 보아 Sst I methylase가 발견된다면 그 specific methylation site는 Alu I methylase의 경우와 달리 internal cytosine이 아닐 것이다. (2) Pvu II와 Sac I endonuclease는 Alu I methylase에 의해 methylation 된 DNA를 전혀 절 단하지 못하는 점으로 보아 Pvu II와 Sac I methylase가 발견된다면 그 specific methylation site는 두 경우 모두 internal cytosine일 가능성이 높다. The cleavage reactions of Hind III, Sst I, Pvu II and Sac I endonucleases were inhibited by the methylation of Alu I methylase. To analyze the cleavage reactions quantitatively, tritium labeled pBR 322 and pPG 3282 plasmid DNAs (pBR 322 DNA contains Hind III and Pvu II sites, while pPG 3282 DNA which is a hog gastrin cDNA clone contains Sst I and Sac I sites) were used, and the degree of the inhibition against cleavages by the four kinds of endonucleases was measured. The results imply that we can predict the specificities of the related hexameric restriction methylases which have not been isolated yet. And the predictions are the followings: (1) The methylation sites of Sst I methylase is not identical with Alu I methylase since Sst I endonuclease slowly cut the sequences methylated by Alu I methylase. (2) The methylation sites of Pvu II and Sac I me thy lases could be identical with Alu I methylase since Pvu II and Sac I endonucleases could not cut the sequences methylated by Alu I methylase.
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Purification and Characterization of Hpa I endonuclease
윤호섭,강선철,유욱준,Yoon, Ho Sup,Kang, Sun Chul,Yoo, Ouk Joon 한국미생물 · 생명공학회 1985 한국미생물·생명공학회지 Vol.13 No.1
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 $2.2{\times}10^6units/mg$이었다. 얻어진 Hpa I endonuclease는 SDS-polyacrylamide gel에서 한개의 band를 보였고, 그 효소활성은 50mM NaCl과 pH 7.0과 7.5사이에서 가장 높았다. 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 $30,000{\pm}1,000$ as judged by 10% polyacrylamide gel electrophoresis containing 0.1% sodium dodesyl sulfate. Hpa I endonuclease was maximally active at neutral pH (7.0 to 7.5) in the presence of 50 mM NaCl.
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제한효소 Hind III , Sst I , Pvu II , Sac I 의 DNA 절단 반응에 있어서 Alu I methylation 의 억제 효과
강선철,윤호섭,유욱준 ( Sun Chul Kang,Ho sup Yoon,Oog . Joon Yoo ) 생화학분자생물학회 1986 BMB Reports Vol.19 No.1
The cleavage reactions of Hind III, Sst I, Pvu II and Sac I endonucleases were inhibited by the methylation of Alu I methylase. To analyze the cleavage reactions quantitatively, tritium labeled pBR 322 and pPG 3282 plasmid DNAs (pBR 322 DNA contains Hind III and Pvu II sites, while pPG 3282 DNA which is a hog gastrin cDNA clone contains Sst I and Sac I sites) were used, and the degree of the inhibition against cleavages by the four kinds of endonucleases was measured. The results imply that we can predict the specificities of the related hexameric restriction methylases which have not been isolated yet. And the predictions are the followings: (1) The methylation sites of Sst I methylase is not identical with Alu I methylase since Sst I endonuclease slowly cut the sequences methylated by Alu I methylase. (2) The methylation sites of Pvu II and Sac I methylases could be identical with ALu I methylase since Pvu II and Sac I endonucleases could not cut the sequences methylated by Alu I methylase.
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