A Restriction Enzyme from Escherichia coli Purification and General Properties | ||
| Engineering and Technology Journal | ||
| Article 1, Volume 27, Issue 5, March 2009, Pages 954-961 PDF (343.73 K) | ||
| DOI: 10.30684/etj.27.5.9 | ||
| Authors | ||
| Mukaram Shikara; Nadia Tariq Barakat; Maysem Modaffer Al-Obaidy | ||
| Abstract | ||
| An endonuclease restriction enzyme has been purified from E. coli about 40-fold with DNAse and RNAse recoveries of about 3%. The purification steps included precipitation of the enzyme with ammonium sulphate, and reclaimed it through Sephadex G-100 and DEAE-cellulose chromatography. The purified endonuclease was able to break lambda DNA into three bands. The enzyme has 5% of carbohydrate moiety which means it is a glycoprotein. Lastly, the comparison with other commercial restriction endonucleases proves that this enzyme is a restriction enzyme with enzymic activity dependent on Mg2+ | ||
| Keywords | ||
| restriction enzyme; Purification; coli; properties | ||
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