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- W219376019 abstract "A new restriction endonuclease, designated as ApaLI, was purified from cell-free extracts of Acetobacter pasteurianus IFO 13753 by streptomycin treatment, ammonium sulfate fractionation, combined column chromatographies on heparin-Sepharose CL-6B and DEAE-Sepharose CL-6B and Fast Protein Liquid Chromatography on Mono Q HR 5/5. The purified enzyme was homogeneous on polyacrylamide gel disc electrophoresis. The molecular weight of the purified enzyme was calculated as 26,000 daltons by gel filtration using Sephadex G-200, and the isoelectric point of the purified enzyme was 4.8 by ampholine sucrose-density gradient isoelectric focusing. The purified enzyme cleaved lambda, Ad2, SV40, M13mp18 RF 1, psi X174 RF I and pBR322 DNAs at 4, 7, 0, 0, 1 and 3 sites, respectively. The purified enzyme worked best at 37 degrees C and pH 8.0 in a reaction mixture (50 microliters) containing 1.0 micrograms lambda DNA, 10mM Tris-HCl, 7 mM 2-mercaptoethanol, 7 mM MgCl2 and 25mM NaCl. However, the purified enzyme did not require NaCl necessarily for the enzyme reaction. The purified enzyme recognized the palindromic hexanucleotide DNA sequence, 5'-GTGCAC-3' and cut between G and T, producing a 5'-cohesive tetranucleotide extension." @default.
- W219376019 created "2016-06-24" @default.
- W219376019 creator A5075092495 @default.
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- W219376019 date "1990-01-01" @default.
- W219376019 modified "2023-10-18" @default.
- W219376019 title "Studies on restriction endonucleases of acetic acid bacteria and allied organisms. Part V. Purification, properties and recognition sequence and cleavage site determinations of restriction endonuclease from acetobacter pasteurianus IFO 13753 (ApaLI)." @default.
- W219376019 cites W2083119773 @default.
- W219376019 doi "https://doi.org/10.1271/bbb1961.54.1791" @default.
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