The cloning, expression and crystallisation of a thermostable arginase
The gene for the thermostable arginase from the thermophilic bacterium ‘ Bacillus caldovelox’ has been cloned and sequenced. Expression of recombinant arginase at high levels has been achieved in E. coli using an inducible T7 RNA polymerase-based system. A facile purification procedure incorporating...
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| Veröffentlicht in: | FEBS letters 1996-05, Vol.386 (2), p.215-218 |
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| container_title | FEBS letters |
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| creator | Bewley, Maria C. Lott, J.Shaun Baker, Edward N. Patchett, Mark L. |
| description | The gene for the thermostable arginase from the thermophilic bacterium ‘
Bacillus caldovelox’ has been cloned and sequenced. Expression of recombinant arginase at high levels has been achieved in
E. coli using an inducible T7 RNA polymerase-based system. A facile purification procedure incorporating a heat-treatment step yielded 0.2 g of recombinant arginase per litre of induced culture. The kinetic properties of the purified recombinant protein are essentially identical to the native enzyme. The recombinant protein has been crystallised and one crystal form is isomorphous to crystals of the native protein. |
| doi_str_mv | 10.1016/0014-5793(96)00459-0 |
| format | Article |
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Bacillus caldovelox’ has been cloned and sequenced. Expression of recombinant arginase at high levels has been achieved in
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Bacillus caldovelox’ has been cloned and sequenced. Expression of recombinant arginase at high levels has been achieved in
E. coli using an inducible T7 RNA polymerase-based system. A facile purification procedure incorporating a heat-treatment step yielded 0.2 g of recombinant arginase per litre of induced culture. The kinetic properties of the purified recombinant protein are essentially identical to the native enzyme. The recombinant protein has been crystallised and one crystal form is isomorphous to crystals of the native protein.</description><subject>Amino Acid Sequence</subject><subject>Arginase</subject><subject>Arginase - chemistry</subject><subject>Arginase - genetics</subject><subject>Arginase - metabolism</subject><subject>Bacillus - enzymology</subject><subject>Bacillus caldovelox</subject><subject>Base Sequence</subject><subject>Cloning, Molecular</subject><subject>Crystallography, X-Ray</subject><subject>DNA, Bacterial</subject><subject>Escherichia coli</subject><subject>Gene cloning</subject><subject>Gene Expression</subject><subject>Hot Temperature</subject><subject>Molecular Sequence Data</subject><subject>Recombinant Fusion Proteins - chemistry</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>Thermophilic</subject><subject>Thermostable</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkFFLwzAUhYMoc07_gUKfRMFqbpo2zYugY1Nh4Mt8Dml6u0W6diadun9va4eP6lO455x7knyEnAK9BgrJDaXAw1jI6EIml5TyWIZ0jwwhFVEY8STdJ8OfyCE58v6VtnMKckAGacIFS-Mhmc6XGJiyrmy1uArwc-3Qe1tXga7ywLitb3RZWq-bTquLQAfNEt2qbvWsxEC7ha20x2NyUOjS48nuHJGX6WQ-fgxnzw9P47tZaLgUNGSSZVCkTArDGWYCcsNyoBJoxjGi2qRMJMww5AiMF3kUccM41TkYZIWBaETO-961q9826Bu1st5gWeoK641XIqWxgPbDfwUhTljMIW6DvA8aV3vvsFBrZ1fabRVQ1XFWHUTVQVSyG1rOirZrZ7v-TbbC_GdpB7b1p73_YUvc_qtTTSf3rDM6XSbfanfRbV-ELdZ3i055Y7EymFuHplF5bX9_6RdnO577</recordid><startdate>19960520</startdate><enddate>19960520</enddate><creator>Bewley, Maria C.</creator><creator>Lott, J.Shaun</creator><creator>Baker, Edward N.</creator><creator>Patchett, Mark L.</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19960520</creationdate><title>The cloning, expression and crystallisation of a thermostable arginase</title><author>Bewley, Maria C. ; 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Bacillus caldovelox’ has been cloned and sequenced. Expression of recombinant arginase at high levels has been achieved in
E. coli using an inducible T7 RNA polymerase-based system. A facile purification procedure incorporating a heat-treatment step yielded 0.2 g of recombinant arginase per litre of induced culture. The kinetic properties of the purified recombinant protein are essentially identical to the native enzyme. The recombinant protein has been crystallised and one crystal form is isomorphous to crystals of the native protein.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>8647285</pmid><doi>10.1016/0014-5793(96)00459-0</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-5793 |
| ispartof | FEBS letters, 1996-05, Vol.386 (2), p.215-218 |
| issn | 0014-5793 1873-3468 |
| language | eng |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Elsevier ScienceDirect Journals; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Arginase Arginase - chemistry Arginase - genetics Arginase - metabolism Bacillus - enzymology Bacillus caldovelox Base Sequence Cloning, Molecular Crystallography, X-Ray DNA, Bacterial Escherichia coli Gene cloning Gene Expression Hot Temperature Molecular Sequence Data Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Sequence Homology, Amino Acid Thermophilic Thermostable |
| title | The cloning, expression and crystallisation of a thermostable arginase |
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