Isolation and enzymatic properties of AtuS Ⅰ methylase = AtuS Ⅰ 메틸화 효소의 분리와 효소적 특성에 관한 연구

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Type II restriction and modification enzymes are an ideal model system for studying specific DNA-protein interaction because of their small size, simple catalytic requirements for activity, and sequence specificity. We chose to study the interaction of the Type II endonuclease and its corresponding methylase from Agrobacterium tumefaciens SSI with DNA. The specific methylase for the recognition site of AtuS I endonuclease from Agrobacterium tumefaciens SSI was purified and its molecular and catalytic properties were studied. For the purification of the enzyme, 20 g of cells were used and disrupted by French press at 20,000 p.s.i.. After ammonium sulfate fractionation, the enzyme was further purified by phophphocellulose column chromatography and DEAE-cellulose column chromatography. The methylase has shown to have the site-specific methylation activity on the AtuS I recognition sequence. ## And AtuS I methylase prefers double-stranded DNA than singlestranded DNA as a substrate. The enzyme showedmaximum activity at values between 7.0 and 8.0 at 37$^\circ$C. and does not essentially require NaCl, $Mg\bar{\cdot}^+$. AtuS I methylation did not inhibit subsequent restriction activities of BstN I and Zan I endonucleases.
Advisors
Yoo, Ook-Joonresearcher유욱준researcher
Description
한국과학기술원 : 생물공학과,
Publisher
한국과학기술원
Issue Date
1988
Identifier
66135/325007 / 000861373
Language
eng
Description

학위논문(석사) - 한국과학기술원 : 생물공학과, 1988.2, [ v, 40 p. ]

Keywords

단백질 분리.

URI
http://hdl.handle.net/10203/28293
Link
http://library.kaist.ac.kr/search/detail/view.do?bibCtrlNo=66135&flag=dissertation
Appears in Collection
BS-Theses_Master(석사논문)
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