PEGylated recombinant L-asparaginase from Erwinia carotovora: Production, properties, and potential applications
N-hydroxysuccinimide ester of monomethoxy polyethylene glycol hemisuccinate was synthesized. It acylated amino groups in a molecule of recombinant L-asparaginase from Erwinia carotovora . A method of L-asparaginase modification by the obtained activated polyethylene glycol derivative was developed....
Gespeichert in:
| Veröffentlicht in: | Applied biochemistry and microbiology 2017-03, Vol.53 (2), p.165-172 |
|---|---|
| Hauptverfasser: | , , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 172 |
|---|---|
| container_issue | 2 |
| container_start_page | 165 |
| container_title | Applied biochemistry and microbiology |
| container_volume | 53 |
| creator | Melik-Nubarov, N. S. Grozdova, I. D. Lomakina, G. Yu Pokrovskaya, M. V. Pokrovski, V. S. Aleksandrova, S. S. Abakumova, O. Yu Podobed, O. V. Grishin, D. V. Sokolov, N. N. |
| description | N-hydroxysuccinimide ester of monomethoxy polyethylene glycol hemisuccinate was synthesized. It acylated amino groups in a molecule of recombinant L-asparaginase from
Erwinia carotovora
. A method of L-asparaginase modification by the obtained activated polyethylene glycol derivative was developed. The best results were produced by modification of the enzyme with a 25-fold excess of reagent relative to the enzyme tetramer. The modified L-asparaginase was isolated from the reaction mixture by gel filtration on Sepharose CL-6B. The purified bioconjugate did not contain PEG unbound to the protein, demonstrated high catalytic activity, and exhibited antiproliferative action on cell cultures. |
| doi_str_mv | 10.1134/S0003683817020119 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_1881749787</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1881749787</sourcerecordid><originalsourceid>FETCH-LOGICAL-c349t-d4e4b963f252ade9104ceb2ef1f3de6dc9156e3e1b3cde332866eb95bb338c563</originalsourceid><addsrcrecordid>eNp1kUFLxDAQhYMouK7-AG8BLx62mjRtmngTWVdhwQX1XNJ0ukS6SU2yyv57U9aDKJ6G4X3v8ZhB6JySK0pZcf1MCGFcMEErkhNK5QGaUE5ExkheHKLJKGejfoxOQnhLq-RCTtCwmi92vYrQYg_abRpjlY14makwKK_WaQ2AO-82eO4_jTUKa-VddB_Oqxu88q7d6micneHBuwF8NBBmWNkWDy6CjUb1WA1Db7QasXCKjjrVBzj7nlP0ej9_uXvIlk-Lx7vbZaZZIWPWFlA0krMuL3PVgqSk0NDk0NGOtcBbLWnJgQFtmG6BsVxwDo0sm4YxoUvOpuhyn5tqvW8hxHpjgoa-VxbcNtRUpFMVshJVQi9-oW9u621ql6iq5FUhyBhI95T2LgQPXT14s1F-V1NSjz-o__wgefK9JyTWrsH_SP7X9AU_bYom</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1875674806</pqid></control><display><type>article</type><title>PEGylated recombinant L-asparaginase from Erwinia carotovora: Production, properties, and potential applications</title><source>SpringerLink Journals</source><creator>Melik-Nubarov, N. S. ; Grozdova, I. D. ; Lomakina, G. Yu ; Pokrovskaya, M. V. ; Pokrovski, V. S. ; Aleksandrova, S. S. ; Abakumova, O. Yu ; Podobed, O. V. ; Grishin, D. V. ; Sokolov, N. N.</creator><creatorcontrib>Melik-Nubarov, N. S. ; Grozdova, I. D. ; Lomakina, G. Yu ; Pokrovskaya, M. V. ; Pokrovski, V. S. ; Aleksandrova, S. S. ; Abakumova, O. Yu ; Podobed, O. V. ; Grishin, D. V. ; Sokolov, N. N.</creatorcontrib><description>N-hydroxysuccinimide ester of monomethoxy polyethylene glycol hemisuccinate was synthesized. It acylated amino groups in a molecule of recombinant L-asparaginase from
Erwinia carotovora
. A method of L-asparaginase modification by the obtained activated polyethylene glycol derivative was developed. The best results were produced by modification of the enzyme with a 25-fold excess of reagent relative to the enzyme tetramer. The modified L-asparaginase was isolated from the reaction mixture by gel filtration on Sepharose CL-6B. The purified bioconjugate did not contain PEG unbound to the protein, demonstrated high catalytic activity, and exhibited antiproliferative action on cell cultures.</description><identifier>ISSN: 0003-6838</identifier><identifier>EISSN: 1608-3024</identifier><identifier>DOI: 10.1134/S0003683817020119</identifier><language>eng</language><publisher>Moscow: Pleiades Publishing</publisher><subject>Biochemistry ; Biomedical and Life Sciences ; Cancer therapies ; Enzymes ; Erwinia carotovora ; Life Sciences ; Medical Microbiology ; Microbiology ; Polyethylene glycol</subject><ispartof>Applied biochemistry and microbiology, 2017-03, Vol.53 (2), p.165-172</ispartof><rights>Pleiades Publishing, Inc. 2017</rights><rights>Applied Biochemistry and Microbiology is a copyright of Springer, 2017.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c349t-d4e4b963f252ade9104ceb2ef1f3de6dc9156e3e1b3cde332866eb95bb338c563</citedby><cites>FETCH-LOGICAL-c349t-d4e4b963f252ade9104ceb2ef1f3de6dc9156e3e1b3cde332866eb95bb338c563</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1134/S0003683817020119$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1134/S0003683817020119$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids></links><search><creatorcontrib>Melik-Nubarov, N. S.</creatorcontrib><creatorcontrib>Grozdova, I. D.</creatorcontrib><creatorcontrib>Lomakina, G. Yu</creatorcontrib><creatorcontrib>Pokrovskaya, M. V.</creatorcontrib><creatorcontrib>Pokrovski, V. S.</creatorcontrib><creatorcontrib>Aleksandrova, S. S.</creatorcontrib><creatorcontrib>Abakumova, O. Yu</creatorcontrib><creatorcontrib>Podobed, O. V.</creatorcontrib><creatorcontrib>Grishin, D. V.</creatorcontrib><creatorcontrib>Sokolov, N. N.</creatorcontrib><title>PEGylated recombinant L-asparaginase from Erwinia carotovora: Production, properties, and potential applications</title><title>Applied biochemistry and microbiology</title><addtitle>Appl Biochem Microbiol</addtitle><description>N-hydroxysuccinimide ester of monomethoxy polyethylene glycol hemisuccinate was synthesized. It acylated amino groups in a molecule of recombinant L-asparaginase from
Erwinia carotovora
. A method of L-asparaginase modification by the obtained activated polyethylene glycol derivative was developed. The best results were produced by modification of the enzyme with a 25-fold excess of reagent relative to the enzyme tetramer. The modified L-asparaginase was isolated from the reaction mixture by gel filtration on Sepharose CL-6B. The purified bioconjugate did not contain PEG unbound to the protein, demonstrated high catalytic activity, and exhibited antiproliferative action on cell cultures.</description><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Cancer therapies</subject><subject>Enzymes</subject><subject>Erwinia carotovora</subject><subject>Life Sciences</subject><subject>Medical Microbiology</subject><subject>Microbiology</subject><subject>Polyethylene glycol</subject><issn>0003-6838</issn><issn>1608-3024</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>BENPR</sourceid><recordid>eNp1kUFLxDAQhYMouK7-AG8BLx62mjRtmngTWVdhwQX1XNJ0ukS6SU2yyv57U9aDKJ6G4X3v8ZhB6JySK0pZcf1MCGFcMEErkhNK5QGaUE5ExkheHKLJKGejfoxOQnhLq-RCTtCwmi92vYrQYg_abRpjlY14makwKK_WaQ2AO-82eO4_jTUKa-VddB_Oqxu88q7d6micneHBuwF8NBBmWNkWDy6CjUb1WA1Db7QasXCKjjrVBzj7nlP0ej9_uXvIlk-Lx7vbZaZZIWPWFlA0krMuL3PVgqSk0NDk0NGOtcBbLWnJgQFtmG6BsVxwDo0sm4YxoUvOpuhyn5tqvW8hxHpjgoa-VxbcNtRUpFMVshJVQi9-oW9u621ql6iq5FUhyBhI95T2LgQPXT14s1F-V1NSjz-o__wgefK9JyTWrsH_SP7X9AU_bYom</recordid><startdate>20170301</startdate><enddate>20170301</enddate><creator>Melik-Nubarov, N. S.</creator><creator>Grozdova, I. D.</creator><creator>Lomakina, G. Yu</creator><creator>Pokrovskaya, M. V.</creator><creator>Pokrovski, V. S.</creator><creator>Aleksandrova, S. S.</creator><creator>Abakumova, O. Yu</creator><creator>Podobed, O. V.</creator><creator>Grishin, D. V.</creator><creator>Sokolov, N. N.</creator><general>Pleiades Publishing</general><general>Springer Nature B.V</general><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PHGZM</scope><scope>PHGZT</scope><scope>PKEHL</scope><scope>PQEST</scope><scope>PQGLB</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope></search><sort><creationdate>20170301</creationdate><title>PEGylated recombinant L-asparaginase from Erwinia carotovora: Production, properties, and potential applications</title><author>Melik-Nubarov, N. S. ; Grozdova, I. D. ; Lomakina, G. Yu ; Pokrovskaya, M. V. ; Pokrovski, V. S. ; Aleksandrova, S. S. ; Abakumova, O. Yu ; Podobed, O. V. ; Grishin, D. V. ; Sokolov, N. N.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c349t-d4e4b963f252ade9104ceb2ef1f3de6dc9156e3e1b3cde332866eb95bb338c563</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Cancer therapies</topic><topic>Enzymes</topic><topic>Erwinia carotovora</topic><topic>Life Sciences</topic><topic>Medical Microbiology</topic><topic>Microbiology</topic><topic>Polyethylene glycol</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Melik-Nubarov, N. S.</creatorcontrib><creatorcontrib>Grozdova, I. D.</creatorcontrib><creatorcontrib>Lomakina, G. Yu</creatorcontrib><creatorcontrib>Pokrovskaya, M. V.</creatorcontrib><creatorcontrib>Pokrovski, V. S.</creatorcontrib><creatorcontrib>Aleksandrova, S. S.</creatorcontrib><creatorcontrib>Abakumova, O. Yu</creatorcontrib><creatorcontrib>Podobed, O. V.</creatorcontrib><creatorcontrib>Grishin, D. V.</creatorcontrib><creatorcontrib>Sokolov, N. N.</creatorcontrib><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest Central (New)</collection><collection>ProQuest One Academic (New)</collection><collection>ProQuest One Academic Middle East (New)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Applied & Life Sciences</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><jtitle>Applied biochemistry and microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Melik-Nubarov, N. S.</au><au>Grozdova, I. D.</au><au>Lomakina, G. Yu</au><au>Pokrovskaya, M. V.</au><au>Pokrovski, V. S.</au><au>Aleksandrova, S. S.</au><au>Abakumova, O. Yu</au><au>Podobed, O. V.</au><au>Grishin, D. V.</au><au>Sokolov, N. N.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>PEGylated recombinant L-asparaginase from Erwinia carotovora: Production, properties, and potential applications</atitle><jtitle>Applied biochemistry and microbiology</jtitle><stitle>Appl Biochem Microbiol</stitle><date>2017-03-01</date><risdate>2017</risdate><volume>53</volume><issue>2</issue><spage>165</spage><epage>172</epage><pages>165-172</pages><issn>0003-6838</issn><eissn>1608-3024</eissn><abstract>N-hydroxysuccinimide ester of monomethoxy polyethylene glycol hemisuccinate was synthesized. It acylated amino groups in a molecule of recombinant L-asparaginase from
Erwinia carotovora
. A method of L-asparaginase modification by the obtained activated polyethylene glycol derivative was developed. The best results were produced by modification of the enzyme with a 25-fold excess of reagent relative to the enzyme tetramer. The modified L-asparaginase was isolated from the reaction mixture by gel filtration on Sepharose CL-6B. The purified bioconjugate did not contain PEG unbound to the protein, demonstrated high catalytic activity, and exhibited antiproliferative action on cell cultures.</abstract><cop>Moscow</cop><pub>Pleiades Publishing</pub><doi>10.1134/S0003683817020119</doi><tpages>8</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0003-6838 |
| ispartof | Applied biochemistry and microbiology, 2017-03, Vol.53 (2), p.165-172 |
| issn | 0003-6838 1608-3024 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_1881749787 |
| source | SpringerLink Journals |
| subjects | Biochemistry Biomedical and Life Sciences Cancer therapies Enzymes Erwinia carotovora Life Sciences Medical Microbiology Microbiology Polyethylene glycol |
| title | PEGylated recombinant L-asparaginase from Erwinia carotovora: Production, properties, and potential applications |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-19T23%3A49%3A14IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=PEGylated%20recombinant%20L-asparaginase%20from%20Erwinia%20carotovora:%20Production,%20properties,%20and%20potential%20applications&rft.jtitle=Applied%20biochemistry%20and%20microbiology&rft.au=Melik-Nubarov,%20N.%20S.&rft.date=2017-03-01&rft.volume=53&rft.issue=2&rft.spage=165&rft.epage=172&rft.pages=165-172&rft.issn=0003-6838&rft.eissn=1608-3024&rft_id=info:doi/10.1134/S0003683817020119&rft_dat=%3Cproquest_cross%3E1881749787%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1875674806&rft_id=info:pmid/&rfr_iscdi=true |