Mukaram Shikara; Nadia Tariq Barakat; Maysem Modaffer Al-Obaidy
Abstract
An endonuclease restriction enzyme has been purified from E. coli about 40-fold withDNAse and RNAse recoveries of about 3%. The purification steps included precipitationof the enzyme ...
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An endonuclease restriction enzyme has been purified from E. coli about 40-fold withDNAse and RNAse recoveries of about 3%. The purification steps included precipitationof the enzyme with ammonium sulphate, and reclaimed it through Sephadex G-100 andDEAE-cellulose chromatography. The purified endonuclease was able to break lambdaDNA into three bands. The enzyme has 5% of carbohydrate moiety which means it is aglycoprotein. Lastly, the comparison with other commercial restriction endonucleasesproves that this enzyme is a restriction enzyme with enzymic activity dependent onMg2+
