Separation/enrichment of active natural low content protein using protein imprinted polymer
We describe a new type of protein-imprinted polymer for separation/enrichment of active natural protein present at a relatively low level in cell extracts, with a cloned bacterial protein as template. In this work, cloned pig cyclophilin 18 (pCyP18) was used as template. The template protein was sel...
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| Veröffentlicht in: | Journal of chromatography. B, Analytical technologies in the biomedical and life sciences Analytical technologies in the biomedical and life sciences, 2008-09, Vol.873 (1), p.113-118 |
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| container_end_page | 118 |
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| container_issue | 1 |
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| container_title | Journal of chromatography. B, Analytical technologies in the biomedical and life sciences |
| container_volume | 873 |
| creator | Han, Ruifang Xing, Xiaocui Wang, Ying Long, Yi Sun, Yang Zhao, Zhuo Mi, Huaifeng |
| description | We describe a new type of protein-imprinted polymer for separation/enrichment of active natural protein present at a relatively low level in cell extracts, with a cloned bacterial protein as template. In this work, cloned pig cyclophilin 18 (pCyP18) was used as template. The template protein was selectively assembled with assistant recognition polymer chains (ARPCs) from their library, which consists of numerous limited length polymer chains with randomly distributed recognition and immobilizing sites. These assemblies of protein and ARPCs were adsorbed by porous polymeric beads and immobilized by cross-linking polymerization. After removing the template, the synthesized imprinted polymer was used to adsorb authentic pCyP18 from cell extract, and its proportional content was enriched 200 times. The assay of peptidyl-prolyl
cis–
trans-isomerase (PPIase) activity showed that natural pCyP18 is more active than cloned pCyP18 and, in particular, it is much more sensitive to the suppressant cyclosporine A (CsA). |
| doi_str_mv | 10.1016/j.jchromb.2008.08.003 |
| format | Article |
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cis–
trans-isomerase (PPIase) activity showed that natural pCyP18 is more active than cloned pCyP18 and, in particular, it is much more sensitive to the suppressant cyclosporine A (CsA).</description><identifier>ISSN: 1570-0232</identifier><identifier>EISSN: 1873-376X</identifier><identifier>DOI: 10.1016/j.jchromb.2008.08.003</identifier><identifier>PMID: 18760974</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>Adsorption ; Analytical, structural and metabolic biochemistry ; Animals ; Assistant recognition polymer chains (ARPCs) ; Bacterial Proteins - chemistry ; Biological and medical sciences ; Cell Extracts - chemistry ; Cloning, Molecular ; Cyclophilin 18 ; Cyclophilins - chemistry ; Cyclophilins - genetics ; Cyclophilins - metabolism ; Fundamental and applied biological sciences. Psychology ; Miscellaneous ; Peptidylprolyl Isomerase - antagonists & inhibitors ; Peptidylprolyl Isomerase - metabolism ; Polymers - chemistry ; PPIase activity ; Protein-imprinted polymer ; Proteins ; Proteins - isolation & purification ; Separation of natural protein ; Swine</subject><ispartof>Journal of chromatography. B, Analytical technologies in the biomedical and life sciences, 2008-09, Vol.873 (1), p.113-118</ispartof><rights>2008 Elsevier B.V.</rights><rights>2008 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c488t-2f50c8c46b8025174c9021d346e616d7e052a02edc798b4863ae31e74400832e3</citedby><cites>FETCH-LOGICAL-c488t-2f50c8c46b8025174c9021d346e616d7e052a02edc798b4863ae31e74400832e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.jchromb.2008.08.003$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,45974</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=20687789$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18760974$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Han, Ruifang</creatorcontrib><creatorcontrib>Xing, Xiaocui</creatorcontrib><creatorcontrib>Wang, Ying</creatorcontrib><creatorcontrib>Long, Yi</creatorcontrib><creatorcontrib>Sun, Yang</creatorcontrib><creatorcontrib>Zhao, Zhuo</creatorcontrib><creatorcontrib>Mi, Huaifeng</creatorcontrib><title>Separation/enrichment of active natural low content protein using protein imprinted polymer</title><title>Journal of chromatography. B, Analytical technologies in the biomedical and life sciences</title><addtitle>J Chromatogr B Analyt Technol Biomed Life Sci</addtitle><description>We describe a new type of protein-imprinted polymer for separation/enrichment of active natural protein present at a relatively low level in cell extracts, with a cloned bacterial protein as template. In this work, cloned pig cyclophilin 18 (pCyP18) was used as template. The template protein was selectively assembled with assistant recognition polymer chains (ARPCs) from their library, which consists of numerous limited length polymer chains with randomly distributed recognition and immobilizing sites. These assemblies of protein and ARPCs were adsorbed by porous polymeric beads and immobilized by cross-linking polymerization. After removing the template, the synthesized imprinted polymer was used to adsorb authentic pCyP18 from cell extract, and its proportional content was enriched 200 times. The assay of peptidyl-prolyl
cis–
trans-isomerase (PPIase) activity showed that natural pCyP18 is more active than cloned pCyP18 and, in particular, it is much more sensitive to the suppressant cyclosporine A (CsA).</description><subject>Adsorption</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Assistant recognition polymer chains (ARPCs)</subject><subject>Bacterial Proteins - chemistry</subject><subject>Biological and medical sciences</subject><subject>Cell Extracts - chemistry</subject><subject>Cloning, Molecular</subject><subject>Cyclophilin 18</subject><subject>Cyclophilins - chemistry</subject><subject>Cyclophilins - genetics</subject><subject>Cyclophilins - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Miscellaneous</subject><subject>Peptidylprolyl Isomerase - antagonists & inhibitors</subject><subject>Peptidylprolyl Isomerase - metabolism</subject><subject>Polymers - chemistry</subject><subject>PPIase activity</subject><subject>Protein-imprinted polymer</subject><subject>Proteins</subject><subject>Proteins - isolation & purification</subject><subject>Separation of natural protein</subject><subject>Swine</subject><issn>1570-0232</issn><issn>1873-376X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1rHSEUhqW0NB_NT2iYTbubm6POqLMKIbRNIZBFWyhkIV7nTONlRm_UScm_r8Md0mXggIrPOb4-hHyksKFAxcVus7MPMUzbDQNQm6WAvyHHVElecyl-vy37VkINjLMjcpLSDoBKkPw9OSqQgE42x-T-B-5NNNkFf4E-Ovswoc9VGCpjs3vCyps8RzNWY_hb2eDzcruPIaPz1Zyc__NyctM-ugL01T6MzxPGD-TdYMaEZ-t6Sn59_fLz-qa-vfv2_frqtraNUrlmQwtW2UZsFbCWysZ2wGjPG4GCil4itMwAw97KTm0bJbhBTlE2Tfk4Z8hPyefD3JLkccaU9eSSxXE0HsOctOhaJpVsC9geQBtDShEHXRJPJj5rCnqxqnd6taoXq3op4KXvfH1g3k7Y_-9aNRbg0wqYZM04ROOtSy8cA6GkVF3hLg8cFh1PDqNO1qG32LuINus-uFei_APMOZk1</recordid><startdate>20080915</startdate><enddate>20080915</enddate><creator>Han, Ruifang</creator><creator>Xing, Xiaocui</creator><creator>Wang, Ying</creator><creator>Long, Yi</creator><creator>Sun, Yang</creator><creator>Zhao, Zhuo</creator><creator>Mi, Huaifeng</creator><general>Elsevier B.V</general><general>Elsevier Science</general><scope>IQODW</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>7X8</scope></search><sort><creationdate>20080915</creationdate><title>Separation/enrichment of active natural low content protein using protein imprinted polymer</title><author>Han, Ruifang ; Xing, Xiaocui ; Wang, Ying ; Long, Yi ; Sun, Yang ; Zhao, Zhuo ; Mi, Huaifeng</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c488t-2f50c8c46b8025174c9021d346e616d7e052a02edc798b4863ae31e74400832e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Adsorption</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Assistant recognition polymer chains (ARPCs)</topic><topic>Bacterial Proteins - chemistry</topic><topic>Biological and medical sciences</topic><topic>Cell Extracts - chemistry</topic><topic>Cloning, Molecular</topic><topic>Cyclophilin 18</topic><topic>Cyclophilins - chemistry</topic><topic>Cyclophilins - genetics</topic><topic>Cyclophilins - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Miscellaneous</topic><topic>Peptidylprolyl Isomerase - antagonists & inhibitors</topic><topic>Peptidylprolyl Isomerase - metabolism</topic><topic>Polymers - chemistry</topic><topic>PPIase activity</topic><topic>Protein-imprinted polymer</topic><topic>Proteins</topic><topic>Proteins - isolation & purification</topic><topic>Separation of natural protein</topic><topic>Swine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Han, Ruifang</creatorcontrib><creatorcontrib>Xing, Xiaocui</creatorcontrib><creatorcontrib>Wang, Ying</creatorcontrib><creatorcontrib>Long, Yi</creatorcontrib><creatorcontrib>Sun, Yang</creatorcontrib><creatorcontrib>Zhao, Zhuo</creatorcontrib><creatorcontrib>Mi, Huaifeng</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of chromatography. 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B, Analytical technologies in the biomedical and life sciences</jtitle><addtitle>J Chromatogr B Analyt Technol Biomed Life Sci</addtitle><date>2008-09-15</date><risdate>2008</risdate><volume>873</volume><issue>1</issue><spage>113</spage><epage>118</epage><pages>113-118</pages><issn>1570-0232</issn><eissn>1873-376X</eissn><abstract>We describe a new type of protein-imprinted polymer for separation/enrichment of active natural protein present at a relatively low level in cell extracts, with a cloned bacterial protein as template. In this work, cloned pig cyclophilin 18 (pCyP18) was used as template. The template protein was selectively assembled with assistant recognition polymer chains (ARPCs) from their library, which consists of numerous limited length polymer chains with randomly distributed recognition and immobilizing sites. These assemblies of protein and ARPCs were adsorbed by porous polymeric beads and immobilized by cross-linking polymerization. After removing the template, the synthesized imprinted polymer was used to adsorb authentic pCyP18 from cell extract, and its proportional content was enriched 200 times. The assay of peptidyl-prolyl
cis–
trans-isomerase (PPIase) activity showed that natural pCyP18 is more active than cloned pCyP18 and, in particular, it is much more sensitive to the suppressant cyclosporine A (CsA).</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>18760974</pmid><doi>10.1016/j.jchromb.2008.08.003</doi><tpages>6</tpages></addata></record> |
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| subjects | Adsorption Analytical, structural and metabolic biochemistry Animals Assistant recognition polymer chains (ARPCs) Bacterial Proteins - chemistry Biological and medical sciences Cell Extracts - chemistry Cloning, Molecular Cyclophilin 18 Cyclophilins - chemistry Cyclophilins - genetics Cyclophilins - metabolism Fundamental and applied biological sciences. Psychology Miscellaneous Peptidylprolyl Isomerase - antagonists & inhibitors Peptidylprolyl Isomerase - metabolism Polymers - chemistry PPIase activity Protein-imprinted polymer Proteins Proteins - isolation & purification Separation of natural protein Swine |
| title | Separation/enrichment of active natural low content protein using protein imprinted polymer |
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