A Restriction Enzyme from Escherichia coli Purification and General Properties

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+

• Publication year

  2009

• Venue

  Engineering and Technology Journal

• Publication date

  2009-03-01

• Fields of study

  Biology, Chemistry

• Identifiers
  DOI 10.30684/etj.27.5.9
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar

• No claims are published for this paper.

• No concepts are published for this paper.

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