Title |
Streptomyces tubercidicus에 존재하는 stu I endonuclease의 정제와 특징 |
Author |
김기태 · 정미영 · 유욱준 |
Address |
한국과학기술원 생물공학과 |
Bibliography |
Korean Journal of Microbiology, 25(3),180-183, 1987 |
DOI |
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Key Words |
Type II restriction endonuclease, Stu I, homogenous preparation |
Abstract |
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±1,000 daltons as judged by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. Stu I endonuclease requires Mg^2+ ion for its activity and is maximally active at neutral pH (7.0-8.0) in the absence of NaCl. |
Download PDF |
Kor_250303_180-183p.pdf |