Molecular imprinting of protein by coordinate interaction
In this article, a novel strong interaction by forming complex between bovine serum albumin (BSA) and copper ion was utilized for the preparation of molecular imprinted hydrogel in aqueous solution. Results show that the inclusion of copper ion in preparation can bridge the template BSA and function...
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| Veröffentlicht in: | Chinese chemical letters 2009-06, Vol.20 (6), p.747-750 |
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| container_title | Chinese chemical letters |
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| creator | Wang, Jun Hua, Zhen Dong Chen, Zhi Yong Li, Yuan Zong Zhao, Mei Ping |
| description | In this article, a novel strong interaction by forming complex between bovine serum albumin (BSA) and copper ion was utilized for the preparation of molecular imprinted hydrogel in aqueous solution. Results show that the inclusion of copper ion in preparation can bridge the template BSA and functional monomers together and improve the imprinting effect compared to the polymer made without copper ion added. High selectivity factor and large adsorption capacity are also observed for the obtained BSA-imprinted hydrogel. |
| doi_str_mv | 10.1016/j.cclet.2008.12.035 |
| format | Article |
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Results show that the inclusion of copper ion in preparation can bridge the template BSA and functional monomers together and improve the imprinting effect compared to the polymer made without copper ion added. High selectivity factor and large adsorption capacity are also observed for the obtained BSA-imprinted hydrogel.</description><identifier>ISSN: 1001-8417</identifier><identifier>EISSN: 1878-5964</identifier><identifier>DOI: 10.1016/j.cclet.2008.12.035</identifier><language>eng</language><publisher>Elsevier B.V</publisher><subject>Bovine serum albumin ; Copper ion ; Molecular imprinted hydrogel</subject><ispartof>Chinese chemical letters, 2009-06, Vol.20 (6), p.747-750</ispartof><rights>2008 Mei Ping Zhao</rights><rights>Copyright © Wanfang Data Co. Ltd. All Rights Reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c335t-cb390d0c4ca2a3a0afd123deb044c7705db6a0e3988385f76760ea450ab3df8f3</citedby><cites>FETCH-LOGICAL-c335t-cb390d0c4ca2a3a0afd123deb044c7705db6a0e3988385f76760ea450ab3df8f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.wanfangdata.com.cn/images/PeriodicalImages/zghxkb/zghxkb.jpg</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.cclet.2008.12.035$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids></links><search><creatorcontrib>Wang, Jun</creatorcontrib><creatorcontrib>Hua, Zhen Dong</creatorcontrib><creatorcontrib>Chen, Zhi Yong</creatorcontrib><creatorcontrib>Li, Yuan Zong</creatorcontrib><creatorcontrib>Zhao, Mei Ping</creatorcontrib><title>Molecular imprinting of protein by coordinate interaction</title><title>Chinese chemical letters</title><description>In this article, a novel strong interaction by forming complex between bovine serum albumin (BSA) and copper ion was utilized for the preparation of molecular imprinted hydrogel in aqueous solution. 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Results show that the inclusion of copper ion in preparation can bridge the template BSA and functional monomers together and improve the imprinting effect compared to the polymer made without copper ion added. High selectivity factor and large adsorption capacity are also observed for the obtained BSA-imprinted hydrogel.</abstract><pub>Elsevier B.V</pub><doi>10.1016/j.cclet.2008.12.035</doi><tpages>4</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1001-8417 |
| ispartof | Chinese chemical letters, 2009-06, Vol.20 (6), p.747-750 |
| issn | 1001-8417 1878-5964 |
| language | eng |
| recordid | cdi_wanfang_journals_zghxkb200906029 |
| source | Access via ScienceDirect (Elsevier); Alma/SFX Local Collection |
| subjects | Bovine serum albumin Copper ion Molecular imprinted hydrogel |
| title | Molecular imprinting of protein by coordinate interaction |
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