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호알칼리성 Coryneform bacteria TU - 19 가 생산하는 세종류의 균체외 단백질분해효소의 정제
강선철,최명철,양재섭 ( Sun Chul Kang,Myoung Chul Choi,Jae Sub Yang ) 한국응용생명화학회 1995 Applied Biological Chemistry (Appl Biol Chem) Vol.38 No.6
Alkalophilic coryneform bacteria TU-19 isolated from soil extracellularly produced at least three proteases (Protease Ⅰ, Ⅱ, and Ⅲ). Investigating the cultural conditions related to the enzyme production of this bacterial cell, the optimum pH and temperature were 10.0 and 30℃, respectively. In order to purify these enzymes from the 2 day culture broth ammonium sulfate fractionation, gel filtration and QAE-Sephadex column chromatography were performed step by step. And then these three proteases were purified to near homogeneity by judging from SDS-PAGE pattern, and had the molecular weights of 120, 80, and 45 kilodaltons, respectively. The optimum pH and temperature for the enzyme activity of Protease Ⅰ and Ⅱ were 10.5 and 45℃, respectively, and Protease Ⅱ were 11.0 and 50℃. And the enzymes were completely inhibited by PMSF suggesting serine protease, but not affected by pCMB. 1,10-phenanthroline, IAA, and EDTA.
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.
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.
농식품 환경 분야(PF) : PF-17 ; 마우스 모델을 이용한 아크릴아마이드 유도된 신독성 및 간독성에 대한 morin hydrate의 보호효과
강선철 ( Sun Chul Kang ),리카자카 ( Rekha Jakhar ),마헨드라 ( Mahendra Pal Singh ) 한국환경농학회 2014 한국환경농학회 학술대회집 Vol.2014 No.-
Acrylamide (AA) is considered as a potential carcinogen by Food and Drug Administration (United States). AA is produced during the heating of starchy foods like potato chips, french fries, and coffee at high temperature and is regarded as a potential genotoxic carcinogen. However, a number of researches going on worldwide in the field of toxicology are concerned about the carcinogenicity of AA. Morin hydrate is a potent flavonoid compound. It is a yellow color substance that can be isolated from Maclura pomifera (Osage orange). So, in this study we have used morin hydrate to abolish the AA-induced toxicity by determining the variety of hematological, biochemical and immunological parameters in the serum, urine, liver and kidney of male mice. Subcutaneous injection of morin hydrate at a concentration of 5mg and 15mg kg-1 per day for 5 days along with 10mg kg-1 AA exposure could significantly reduce the toxicity of AA. As we found a significant reduction in the level of thiobarbituric reactive substances (TBARS) in tissue and serum, also, a significant reduction in antioxidant enzymes like superoxide dismutase (SOD), glutathione S transferase (GST), glutathione (GSH), myeloperoxidase (MPO) was observed. On the other hand, level of aspartate amino transferase (AST), alinine aminotransferase (ALT) in serum was found to decrease in a concentration dependent manner of morin hydrate. On the basis of the present study we conclude that morin hydrate can potentially protect renal and hepatic toxicity induced by AA.