• Journal of Microbiology and Biotechnology
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• v.5 no.5
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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.

• Proceedings of the Korean Society of Life Science Conference
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• 2008.10a
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• pp.79.1-79.1
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• 2008

• Proceedings of the PSK Conference
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• 2000.10a
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• pp.203.1-203.1
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• 2000

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• 2001.05a
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• pp.96-96
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• 2001

• Proceedings of the Korean Society of Applied Entomolohy Conference
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• 2001.05a
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• pp.103-103
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• 2001

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• 2001.11a
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• pp.119-119
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• 2001

• Proceedings of the Korean Society of Life Science Conference
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• 2005.04a
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• pp.125-125
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• 2005

• Proceedings of the Korean Society of Life Science Conference
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• 2006.09a
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• pp.110.1-110.1
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• 2006

• Proceedings of the Korean Society of Life Science Conference
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• 2005.04a
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• pp.127-127
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• 2005

• Proceedings of the Zoological Society Korea Conference
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• 2000.10a
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• pp.288.2-289
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• 2000

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