Literature DB >> 1300999

[BspLS2I--a new site-specific endonuclease from the thermophilic bacteria Bacillus species LS2].

N P Kovalevskaia, L A Zheleznaia, N I Matvienko.   

Abstract

A new restriction endonuclease BspLS2I was isolated from the thermophilic bacterium Bacillus species LS2 and purified by blue sepharose and hydroxyapatite chromatographies. The enzyme is an isoschizomer of SduI from Streptococcus durans. BspLS2I recognizes the sequence 5' G(G/A/T)GC(C/T/A) decreases C 3' on double-stranded DNA and cleaves it is indicated by the arrow to yield sticky-ended DNA fragments. Maximum catalytic activity of endonuclease was found in 10 mM tris-HCl (pH 7.9) in the presence of 15-30 mM MgCl2 at 50 degrees C. The phage T4 glucosylated DNA is not cleaved by the enzyme.

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Year:  1992        PMID: 1300999

Source DB:  PubMed          Journal:  Bioorg Khim        ISSN: 0132-3423


  1 in total

1.  REBASE--restriction enzymes and methylases.

Authors:  R J Roberts; D Macelis
Journal:  Nucleic Acids Res       Date:  1993-07-01       Impact factor: 16.971

  1 in total

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