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KMID : 0364819880260010001
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Korean Journal of Microbiology
1988 Volume.26 No. 1 p.1 ~ p.5
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Characterization of Bmal endonuclease from Bacillus macerans ATCC 8244
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Kwon, Y.T./권용태
Jun, H.S./Rho, H.M./전희숙/노현모
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Abstract
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1
The isolation and characterization of a new type II restriction endonuclease, BmaI, from Bacillus macerans ATCC 8244 were described. Bmal endonuclease was partially purified by procedures of ammonium sulfate fractionation, DEAE-cellulose and phosphocellulose chromatographies. This enzyme recognized one site on pBR322 DNA, two sites on Bluescribe DNA, three sites on ADNA and no site on SV 40 DNA. The same cleavage patterns for various DNAs as Pvul indicated that BmaI is an isoschisomer of Pvul whose recognition sequence is 5´-CGATCG3´. The optimal pH for the Bmal endonuclease activity was about 7.0 and optimal NaCl concentration was about 100 mM. Manganese ion could partially replace magnesium as a cofactor, but calcium could not at all.
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