Characterization of BmaI endonuclease from bacillus macerans ATCC 8244

Bacillus macerans의 BmaI endonuclease의 특성에 대한 연구

  • 권용태 (서울대학교 자연과학대학 동물학과 분자유전학실) ;
  • 전희숙 (서울대학교 자연과학대학 동물학과 분자유전학실) ;
  • 노현모 (서울대학교 자연과학대학 동물학과 분자유전학실)
  • Published : 1988.03.01


The esolation and characterization of a new type II restriction endounclease, BamI, from Bacellus macerans ATCC 8244 were described. BmaI endonuclease was partially purified by procedures of ammonium sulfate fractionation, DEAE-cellulose and phosphocellulose chromatographies. This enzume recognized one site on pBR322 DNA, two sites on Bluescribe DNA, three sites on $\lambda$DNA and no site on SV 40 DNA. The same cleavage patterns for vareius DNAs as PvuI indicated that BamI is an isoschisomer of PvuI whose recognition sequence is 5'-CGATCG-3'. The optimal pH for the BmaI endonuclease activity was about 7.0 and optimal NaCl concentration was about 100mM. Manganese ion could partially replace magnesium as a cofactor, but calcium could not at all.