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Nucleic Acids Research, 1992, Vol. 20, No. 3 433-438
© 1992

ENZYMOLOGY

Purification and properties of the Mboll, a class-IIs restriction endonuclease

Marian Sektas, Tadeusz Kaczorowski and Anna J. Podhajska*

Department of Microbiology, University of Gdansk Kladki 24, 80-822 Gdansk, Poland

*To whom correspondence should be addressed

Received November 14, 1991. Accepted February 10, 1992.

After five purification steps a homogeneous preparation of endonuclease Mboll was obtained, and several properties of the enzyme were determined. Mboll is a monomer, with Mr under native and denaturing conditions being 47 – 49 x 103 Da. Endonuclease Mboll is a basic protein (pl 8.3) which remains active when Mg2+ is replaced by Mn2+, Co2+, Ca2+, or Fe2+. Mboll exhibits a star activity in the presence of some of the following reagents or ions: DMSO, glycerol, ethanol (and Co2+ or Mn2+ at pH 6). MboII does not bend DNA and is heat sensitive, losing activity after 15 min at 50°C.


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