A Restriction Enzyme from Escherichia coli Purification and General Properties
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 endonu...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
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Unviversity of Technology- Iraq
2009-03-01
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| Series: | Engineering and Technology Journal |
| Subjects: | |
| Online Access: | https://etj.uotechnology.edu.iq/article_29309_4b1b6f4648f4387c4cdf6146dfff1428.pdf |
| Summary: | 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+ |
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| ISSN: | 1681-6900 2412-0758 |