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KMID : 0364819870250030180
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Korean Journal of Microbiology
1987 Volume.25 No. 3 p.180 ~ p.183
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Purification and Characterization of Stu I Endonuclease from Streptomyces Tubercidicus
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Kim, Ki Tae/김기태
Jung, Mi Young/Yoo, Ook Joun/정미영/유욱준
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Abstract
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1
Stu I, a type II restriction endonuclease, has been purified to homogeneity from Streptomyces tubercidicus (ATCC 25502), and its catalytic properties have been studied. For the purification of Stu I endonuclease free of nonspecific nucleases, DEAE-Sephadex (A-50), QAE-Sephadex (A-50) and Heparin-agarose column chromatography have been performed after ammonium sulfate fractionation of the crude extract. The enzyme was further purified by gel filtration using Sephadex G-100 column to obtain homogeneous form of protein.
The single polypeptide species of Stu I endonuclease has a subunit molecular weight of 34,000 t 1,000 daltons as judged by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate.
Stu I endonuclease requires Mgt+ ion for its activity and is maximally active at neutral pH (7.0-8.0) in the absence of NaCl.
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