(The) purification and characterization of a new type Ⅱ restriction endonuclease, XciⅠ = XciⅠ 제한 효소의 정제 및 분자적 특성에 관한 연구

TypeII restriction and modification enzymes are ideal model systems for studying the specific DNA-protein interaction because of their small size, simple catalytic requirements for activity and recognition sequence specificity. A new restriction endonuclease, XciI, has been partially purified from Xanthomonas citri IFO 3835, it catalytic properties and recognition sequence have been identified. This enzyme XciI cleaves bacteriophage $\lambda$DNA at two sites, pUC9 and pBR322 plasmid DNA at one site, but it cleaves neither $\phi$X174 DNA nor SV40 DNA. The enzyme shows maximum activity at pH values between 7.5 and 9.0, and in the presence of 20 mM MgCl$_2$. The addition of large amounts of Sodium Chloride ($>100mM$) causes a decrease in XciI activity. Temperature for optimum endonuclease activity is $37\,^\circ\!C$. But, Bovine Serum Albumin and sulfhydryl compounds have no influences on XciI restriction endonuclease activity. This restriction endonuclease XciI recognizes the sequence 5``-GTCGAC-3`` 3``-CAGCTG-5`` and cuts at the sites indicated by the arrows, identical with that cleaved by endonuclease SaII (of Streptomyces albus G).
Advisors
Yoo, Ook-Joonresearcher유욱준researcher
Publisher
한국과학기술원
Issue Date
1985
Identifier
64513/325007 / 000831444
Language
eng
Description

학위논문(석사) - 한국과학기술원 : 생물공학과, 1985.2, [ 43 p. ]

Keywords

단백질 분리.

URI
http://hdl.handle.net/10203/28222
Link
http://library.kaist.ac.kr/search/detail/view.do?bibCtrlNo=64513&flag=t
Appears in Collection
BS-Theses_Master(석사논문)
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