Authors
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
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