[Specific endonuclease BbvBI from Bacillus brevis].
A new restriction endonuclease BbvBI free from contaminating nonspecific nucleases and phosphatases was isolated from the Bacillus brevis cells. The enzyme was purified by fractionating the sonicated cell-free extract in a two-phase PEG/dextran system and subsequent chromatographies on DEAE-sepharose, blue sepharose and heparin sepharose. The endonuclease BbvBI displayed the maximal activity at 45 degrees C, pH between 8.0 and 8.5, MgCl2 concentration in the range of 5-10 mM and at the low ionic strength. It is shown that the enzyme cleaves the sequence G'GYPC'C, with the preferential cleavage of GGTACC and GGCACC sites as compared with GGTGCC and GGCGCC. Thus, the restriction endonuclease BbvBI is a true isoschizomer of nuclease BanI.
Sokolov
N N
NN
El'darov
M A
MA
Anikeĭcheva
N V
NV
Karpychev
I V
IV
Samko
O T
OT
Fitsner
A B
AB
Kalugin
A A
AA
Khoroshutina
E B
EB
Skriabin
K G
KG
D001407:Bacillus / Q000201:enzymology*; D002853:Chromatography, Liquid; D004262:DNA Restriction Enzymes / Q000302:isolation & purification / Q000378:metabolism*; D004587:Electrophoresis, Agar Gel; D006863:Hydrogen-Ion Concentration; D009994:Osmolar Concentration; D013379:Substrate Specificity
D004262:DNA Restriction Enzymes
Spetsificheskaia éndonukleza BbvBI iz Bacillus brevis.