title: Site-specific endonuclease from thermophilic Bacillus species MK strain is isoschizomer of SalI.
abstract: Screening of thermophilic bacterial strains revealed a strain containing site-specific endonuclease BspMKI. This endonuclease was purified to functional homogeneity during sequential chromatographic steps. The enzyme recognizes sequence 5'-G decreases TCGAC-3' on DNA molecule and is isoschizomer of endonuclease SalI. The molecular mass of BspMKI is about 45 kD. The enzyme is maximally active at 55 degrees C and MRB (50 mM NaCl, 10 mM Tris-HCl, pH 7.4, 10 mM MgCl2, 1 mM dithiothreitol) is the optimal buffer. The enzyme is highly stable and retains its activity during two weeks at room temperature.
authors.affiliation: Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, Russia. protres@sovam.com
authors.forename: M A
authors.initials: MA
authors.lastname: Kerzhner
authors.forename: S A
authors.initials: SA
authors.lastname: Shiryaev
authors.forename: L A
authors.initials: LA
authors.lastname: Zheleznaya
authors.forename: N I
authors.initials: NI
authors.lastname: Matvienko
mesh_terms: D001407:Bacillus / Q000201:enzymology*; D004247:DNA / Q000378:metabolism; D015252:Deoxyribonucleases, Type II Site-Specific / Q000378:metabolism*; D006868:Hydrolysis; D008970:Molecular Weight; D013379:Substrate Specificity
chemical_list: D004247:DNA; D015252:Deoxyribonucleases, Type II Site-Specific; C029792:GTCGAC-specific type II deoxyribonucleases