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...
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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 |
| _version_ | 1797325230000046080 |
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| author | Mukaram Shikara Nadia Tariq Barakat Maysem Modaffer Al-Obaidy |
| author_facet | Mukaram Shikara Nadia Tariq Barakat Maysem Modaffer Al-Obaidy |
| author_sort | Mukaram Shikara |
| collection | DOAJ |
| description | 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+ |
| first_indexed | 2024-03-08T06:06:35Z |
| format | Article |
| id | doaj.art-6b29c355a6734a9fa696b1949480cea6 |
| institution | Directory Open Access Journal |
| issn | 1681-6900 2412-0758 |
| language | English |
| last_indexed | 2024-03-08T06:06:35Z |
| publishDate | 2009-03-01 |
| publisher | Unviversity of Technology- Iraq |
| record_format | Article |
| series | Engineering and Technology Journal |
| spelling | doaj.art-6b29c355a6734a9fa696b1949480cea62024-02-04T17:49:12ZengUnviversity of Technology- IraqEngineering and Technology Journal1681-69002412-07582009-03-0127595496110.30684/etj.27.5.929309A Restriction Enzyme from Escherichia coli Purification and General PropertiesMukaram ShikaraNadia Tariq BarakatMaysem Modaffer Al-ObaidyAn 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+https://etj.uotechnology.edu.iq/article_29309_4b1b6f4648f4387c4cdf6146dfff1428.pdfrestriction enzymepurificationcoliproperties |
| spellingShingle | Mukaram Shikara Nadia Tariq Barakat Maysem Modaffer Al-Obaidy A Restriction Enzyme from Escherichia coli Purification and General Properties Engineering and Technology Journal restriction enzyme purification coli properties |
| title | A Restriction Enzyme from Escherichia coli Purification and General Properties |
| title_full | A Restriction Enzyme from Escherichia coli Purification and General Properties |
| title_fullStr | A Restriction Enzyme from Escherichia coli Purification and General Properties |
| title_full_unstemmed | A Restriction Enzyme from Escherichia coli Purification and General Properties |
| title_short | A Restriction Enzyme from Escherichia coli Purification and General Properties |
| title_sort | restriction enzyme from escherichia coli purification and general properties |
| topic | restriction enzyme purification coli properties |
| url | https://etj.uotechnology.edu.iq/article_29309_4b1b6f4648f4387c4cdf6146dfff1428.pdf |
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