• Journal of Microbiology and Biotechnology
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• 제5권5호
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• pp.269-273
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• 1995

A thermotolerable restriction endonuclease. Svil, found in Streptomyces violochromogenes D2-5 was purified. For the purification, streptomycin sulfate and ammonium sulfate precipitation was used. Ph osphocellulose P-ll, DEAE-Cellulose and Sephacryl-S200 HR colum chromatography were also performed. The purified enzyme was found to be homogeneous and the molecular weight of the enzyme estimated by polyacrylamide gel electrophoresis containing 0.1$%$ SDS was about 32, 000 daltons. The recognition sequence and cleavage site of the enzyme were determined to be $5^1$-$TT\downarrow CGAA$-$3^1$ which is the same sequence as that of Asull. Unlike Asull, however, the Svil shows high thermal stability.

• 한국생명과학회:학술대회논문집
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• 한국생명과학회 2008년도 제49회 학술심포지움 및 국제학술대회
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• pp.79.1-79.1
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• 2008

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• 대한약학회 2000년도 NEW STRATEGY FOR DRUG DEVELOPMENT IN POST-GENOMIC ERA(대한약학회)
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• 2000

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• 2001

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• 2001

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• 2001

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• pp.125-125
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• 2005

• 한국생명과학회:학술대회논문집
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• pp.110.1-110.1
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• 2006

• 한국생명과학회:학술대회논문집
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• 한국생명과학회 2005년도 국제학술심포지움 The 44th Annual Meeting of Korean Society for Life Science
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• pp.127-127
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• 2005

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• pp.288.2-289
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• 2000

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