title: Purification and characterization of the FokI restriction endonuclease.
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+.
authors.affiliation: Department of Microbiology, University of Gdańsk, Poland.
authors.forename: T
authors.initials: T
authors.lastname: Kaczorowski
authors.forename: P
authors.initials: P
authors.lastname: Skowron
authors.forename: A J
authors.initials: AJ
authors.lastname: Podhajska
mesh_terms: D002413:Cations, Divalent; D002845:Chromatography / Q000379:methods; D015252:Deoxyribonucleases, Type II Site-Specific / Q000302:isolation & purification*; D005417:Flavobacterium / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D008970:Molecular Weight; D011487:Protein Conformation; D012492:Salts; D013696:Temperature
chemical_list: D002413:Cations, Divalent; D012492:Salts; C035042:endodeoxyribonuclease FokI; D015252:Deoxyribonucleases, Type II Site-Specific