A restriction enzyme from escherichia coli purification and general properties

الملخص EN

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+-