An activated medium with high durability and low nonspecific adsorption: Application to protein A chromatography
Activated media allow the user to easily synthesize a variety of affinity media. We have developed a novel activated medium based on porous silica modified with phosphorylcholine (PC) and N-hydroxysuccinimide (NHS) groups for the purpose of high-throughput purification and reducing nonspecific prote...
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| Veröffentlicht in: | Analytical biochemistry 2011-02, Vol.409 (1), p.123-129 |
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| container_title | Analytical biochemistry |
| container_volume | 409 |
| creator | Maeno, Katsuyuki Hirayama, Aya Sakuma, Kenichi Miyazawa, Kazuyuki |
| description | Activated media allow the user to easily synthesize a variety of affinity media. We have developed a novel activated medium based on porous silica modified with phosphorylcholine (PC) and
N-hydroxysuccinimide (NHS) groups for the purpose of high-throughput purification and reducing nonspecific protein adsorption. The PC groups function as suppressors of nonspecific protein adsorption, whereas the NHS groups are able to covalently bind to the primary amino groups of ligands. Because protein A affinity medium is the most frequently used affinity medium, we prepared protein A media in which a recombinant protein A was bound to the NHS groups of the activated media and evaluated its utility. After optimizing various factors in the synthetic process, the resultant protein A medium showed improved durability at a high flow rate over 300 purification cycles and reduced nonspecific protein adsorption compared with commercially available protein A media. |
| doi_str_mv | 10.1016/j.ab.2010.10.001 |
| format | Article |
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N-hydroxysuccinimide (NHS) groups for the purpose of high-throughput purification and reducing nonspecific protein adsorption. The PC groups function as suppressors of nonspecific protein adsorption, whereas the NHS groups are able to covalently bind to the primary amino groups of ligands. Because protein A affinity medium is the most frequently used affinity medium, we prepared protein A media in which a recombinant protein A was bound to the NHS groups of the activated media and evaluated its utility. After optimizing various factors in the synthetic process, the resultant protein A medium showed improved durability at a high flow rate over 300 purification cycles and reduced nonspecific protein adsorption compared with commercially available protein A media.</description><subject>Adsorption</subject><subject>Affinity</subject><subject>Chromatography, Affinity - methods</subject><subject>High throughput</subject><subject>Nonspecific</subject><subject>Phosphorylcholine</subject><subject>Phosphorylcholine - chemistry</subject><subject>Protein A</subject><subject>Protein Binding</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>Silicon Dioxide - chemistry</subject><subject>Staphylococcal Protein A - chemistry</subject><subject>Staphylococcal Protein A - genetics</subject><subject>Staphylococcal Protein A - metabolism</subject><subject>Succinimides - chemistry</subject><issn>0003-2697</issn><issn>1096-0309</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kD1v2zAQhokiQeOm3TsV3DrJPeqLYjYjSJsCAbIkM3EiKYuGJKokZcP_vnTtdMt0uMNzL-4eQr4yWDNg9Y_dGtt1Dv_aNQD7QFYMRJ1BAeKKrACgyPJa8BvyKYRdAlhZ1R_JTQ6iYjWHFZk3E0UV7R6j0XQ02i4jPdjY095ue6oXj60dbDxSnDQd3IFObgqzUbaziqIOzs_RuumObuZ5sApPDY2Ozt5FYye6oar3bsToth7n_viZXHc4BPPlUm_J68-Hl_vH7On51-_7zVOmilLEDDkKRM6bjomiraDoeF01XVMrXSAvS82xA17Vpca2EZjeyYum1SU0CgTvWHFLvp9z0yF_FhOiHG1QZhhwMm4JsskZE2WykEg4k8q7ELzp5OztiP4oGciTZrmT2MqT5tMkWUwr3y7hS5uc_V9485qAuzNg0ot7a7wMyppJJb_eqCi1s--n_wVPjY2w</recordid><startdate>20110201</startdate><enddate>20110201</enddate><creator>Maeno, Katsuyuki</creator><creator>Hirayama, Aya</creator><creator>Sakuma, Kenichi</creator><creator>Miyazawa, Kazuyuki</creator><general>Elsevier Inc</general><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>20110201</creationdate><title>An activated medium with high durability and low nonspecific adsorption: Application to protein A chromatography</title><author>Maeno, Katsuyuki ; Hirayama, Aya ; Sakuma, Kenichi ; Miyazawa, Kazuyuki</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c349t-a7a9aa778f193b503f7658f86cd3a744d7af07564dab89a951238bd408c097f13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Adsorption</topic><topic>Affinity</topic><topic>Chromatography, Affinity - methods</topic><topic>High throughput</topic><topic>Nonspecific</topic><topic>Phosphorylcholine</topic><topic>Phosphorylcholine - chemistry</topic><topic>Protein A</topic><topic>Protein Binding</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - metabolism</topic><topic>Silicon Dioxide - chemistry</topic><topic>Staphylococcal Protein A - chemistry</topic><topic>Staphylococcal Protein A - genetics</topic><topic>Staphylococcal Protein A - metabolism</topic><topic>Succinimides - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Maeno, Katsuyuki</creatorcontrib><creatorcontrib>Hirayama, Aya</creatorcontrib><creatorcontrib>Sakuma, Kenichi</creatorcontrib><creatorcontrib>Miyazawa, Kazuyuki</creatorcontrib><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>Analytical biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Maeno, Katsuyuki</au><au>Hirayama, Aya</au><au>Sakuma, Kenichi</au><au>Miyazawa, Kazuyuki</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>An activated medium with high durability and low nonspecific adsorption: Application to protein A chromatography</atitle><jtitle>Analytical biochemistry</jtitle><addtitle>Anal Biochem</addtitle><date>2011-02-01</date><risdate>2011</risdate><volume>409</volume><issue>1</issue><spage>123</spage><epage>129</epage><pages>123-129</pages><issn>0003-2697</issn><eissn>1096-0309</eissn><abstract>Activated media allow the user to easily synthesize a variety of affinity media. We have developed a novel activated medium based on porous silica modified with phosphorylcholine (PC) and
N-hydroxysuccinimide (NHS) groups for the purpose of high-throughput purification and reducing nonspecific protein adsorption. The PC groups function as suppressors of nonspecific protein adsorption, whereas the NHS groups are able to covalently bind to the primary amino groups of ligands. Because protein A affinity medium is the most frequently used affinity medium, we prepared protein A media in which a recombinant protein A was bound to the NHS groups of the activated media and evaluated its utility. After optimizing various factors in the synthetic process, the resultant protein A medium showed improved durability at a high flow rate over 300 purification cycles and reduced nonspecific protein adsorption compared with commercially available protein A media.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>20951670</pmid><doi>10.1016/j.ab.2010.10.001</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Analytical biochemistry, 2011-02, Vol.409 (1), p.123-129 |
| issn | 0003-2697 1096-0309 |
| language | eng |
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| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Adsorption Affinity Chromatography, Affinity - methods High throughput Nonspecific Phosphorylcholine Phosphorylcholine - chemistry Protein A Protein Binding Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Silicon Dioxide - chemistry Staphylococcal Protein A - chemistry Staphylococcal Protein A - genetics Staphylococcal Protein A - metabolism Succinimides - chemistry |
| title | An activated medium with high durability and low nonspecific adsorption: Application to protein A chromatography |
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