Title Brevibacterium divaricatum의 제한효소 Bdi I의 특성
Author 김용석 · 노현모
Address 서울대학교 자연과학대학 동물학과
Bibliography Korean Journal of Microbiology, 24(1),18-23, 1986
DOI
Key Words Characterization of the restriction endonuclease Bki I from brevibacterium divaricatum
Abstract A new type II restriction endonuclease, Bdi I, has been isolated from Brenibacterium divaricatum FERM 5948 by procedures of ammonium sulfate fractionation, DEAE-cellulose chromatography and heparin agarose chromatography. The purified Bdi I restriction endonudlease had the same cleavage patterns of Cla I whose recognition sequence is 5' ATCGAT 3'. From the result that λ-Cla I DNA fragment could be cloned in pBR 322 digested with Bdi I, it has been proven that Bdi I cuts between T and C(5' AT/CGAT3') within the recognition sequence and produces 5'pCG cohesive end. The optimal temperature for the Bdi I restriction endonuclease activity was 37.deg.C, and optimal salt (NaCl) concentration was 50-100 mM.
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