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. 1989 Aug 15;80(2):209-16.
doi: 10.1016/0378-1119(89)90285-0.

Purification and characterization of the FokI restriction endonuclease

T Kaczorowski  1 , P Skowron, A J Podhajska
Affiliations

Purification and characterization of the FokI restriction endonuclease

T Kaczorowski et al. Gene. .

Abstract

The restriction endonuclease FokI from Flavobacterium okeanokoites was purified to homogeneity. Based on gel filtration, sedimentation and sodium dodecyl sulfate-polyacrylamide-gel electrophoresis, the following properties of the enzyme were determined: FokI exists in one active monomeric form, and has an Mr of 64-65.4 x 10(3).FokI is a strongly basic protein with an isoelectric point of 9.4. The enzyme exhibits restriction activity in the pH range 5.0 to 10.5 (maximum level at pH 7.0-8.5) and its divalent cation requirement is satisfied not only by Mg2+, but also by Co2+, Mn2+, Ni2+, Cd2+, Zn2+ and Fe2+.

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