title: Purification and characterisation of Bst LVI restriction endonuclease, a thermostable isoschizomer of ClaI from Bacillus stearothermophilus LV.
abstract: This work describes the purification and biochemical characterization of BstLVI restriction endonuclease, a thermostable isoschizomer of ClaI, from Bacillus stearothermophilus LV. The enzyme was purified by successive DEAE-cellulose, Affi-Gel Blue and Heparin-Sepharose CL-6B column chromatography. A molecular weight of 37,000 was determined for Bst LVI by gel filtration. As expected from thermophilic proteins, the enzyme showed a high stability towards heat and also to other known protein-denaturing agents.
authors.affiliation: Departamento de Ciencias Biológicas, Universidad de Talca, Chile.
authors.forename: C
authors.initials: C
authors.lastname: Lobos
authors.forename: C
authors.initials: C
authors.lastname: Vásquez
mesh_terms: D004247:DNA / Q000378:metabolism; D015252:Deoxyribonucleases, Type II Site-Specific / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D004795:Enzyme Stability; D001411:Geobacillus stearothermophilus / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D004247:DNA; C032824:ATCGAT-specific type II deoxyribonucleases; D015252:Deoxyribonucleases, Type II Site-Specific