Preparation and development of anti-chitosan antibodies
Polyclonal antibodies directed against chitosan were produced using several immunogens, prepared by binding the polymer according to two ways (covalent and electrostatic) with a protein (bovine serum albumin or hemocyanin). It appeared that the presence of a carrier protein linked to chitosan was ne...
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Veröffentlicht in: | Journal of biomedical materials research 2003-12, Vol.67A (3), p.766-774 |
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description | Polyclonal antibodies directed against chitosan were produced using several immunogens, prepared by binding the polymer according to two ways (covalent and electrostatic) with a protein (bovine serum albumin or hemocyanin). It appeared that the presence of a carrier protein linked to chitosan was necessary to enhance the immune response and to obtain antibodies in a stable and reproducible way. Direct and inhibition enzyme‐linked immunosorbent assay experiments were performed to assess the affinity and the specificity of the antibodies. The interactions of these antibodies with modified chitosans showed no influence of the degree of polymerization of the polymer in the range studied (from 24 to 2261), by contrast with the degree of acetylation. The affinity decreased when the degree of acetylation increased. Absence of cross‐reactivity with glycosaminoglycans was observed whatever the antibody. The cationicity of the amine function along the polymer chains may have a role in the immunological recognition of the chitosan structure. © 2003 Wiley Periodicals, Inc. J Biomed Mater Res 67A: 766–774, 2003 |
doi_str_mv | 10.1002/jbm.a.10132 |
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It appeared that the presence of a carrier protein linked to chitosan was necessary to enhance the immune response and to obtain antibodies in a stable and reproducible way. Direct and inhibition enzyme‐linked immunosorbent assay experiments were performed to assess the affinity and the specificity of the antibodies. The interactions of these antibodies with modified chitosans showed no influence of the degree of polymerization of the polymer in the range studied (from 24 to 2261), by contrast with the degree of acetylation. The affinity decreased when the degree of acetylation increased. Absence of cross‐reactivity with glycosaminoglycans was observed whatever the antibody. The cationicity of the amine function along the polymer chains may have a role in the immunological recognition of the chitosan structure. © 2003 Wiley Periodicals, Inc. J Biomed Mater Res 67A: 766–774, 2003</description><identifier>ISSN: 1549-3296</identifier><identifier>ISSN: 0021-9304</identifier><identifier>EISSN: 1552-4965</identifier><identifier>EISSN: 1097-4636</identifier><identifier>DOI: 10.1002/jbm.a.10132</identifier><identifier>PMID: 14613224</identifier><identifier>CODEN: JBMRBG</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Acetylation ; Animals ; Antibodies - immunology ; Antibodies - isolation & purification ; Antibody Affinity ; Antibody Formation ; Antibody Specificity ; Biological and medical sciences ; Carrier Proteins ; Chitin - analogs & derivatives ; Chitin - immunology ; Chitosan ; Decapodiformes ; degree of acetylation ; ELISA ; glycosaminoglycans ; hemocyanin ; Hemocyanins ; Medical sciences ; Molecular Weight ; polyclonal antibodies ; Protein Binding ; Rabbits ; Radiotherapy. Instrumental treatment. Physiotherapy. Reeducation. Rehabilitation, orthophony, crenotherapy. Diet therapy and various other treatments (general aspects) ; Serum Albumin, Bovine ; Technology. Biomaterials. Equipments. Material. Instrumentation</subject><ispartof>Journal of biomedical materials research, 2003-12, Vol.67A (3), p.766-774</ispartof><rights>Copyright © 2003 Wiley Periodicals, Inc.</rights><rights>2004 INIST-CNRS</rights><rights>Copyright 2003 Wiley Periodicals, Inc. J Biomed Mater Res 67A: 766-774, 2003</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5342-8184e656fb109adabed8b12ec22163ce9e9448c50d1222e375e16675ac3778af3</citedby><cites>FETCH-LOGICAL-c5342-8184e656fb109adabed8b12ec22163ce9e9448c50d1222e375e16675ac3778af3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fjbm.a.10132$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fjbm.a.10132$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=15328833$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14613224$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sorlier, Pierre</creatorcontrib><creatorcontrib>Hartmann, Daniel J.</creatorcontrib><creatorcontrib>Denuzière, Anne</creatorcontrib><creatorcontrib>Viton, Christophe</creatorcontrib><creatorcontrib>Domard, Alain</creatorcontrib><title>Preparation and development of anti-chitosan antibodies</title><title>Journal of biomedical materials research</title><addtitle>J. Biomed. Mater. Res</addtitle><description>Polyclonal antibodies directed against chitosan were produced using several immunogens, prepared by binding the polymer according to two ways (covalent and electrostatic) with a protein (bovine serum albumin or hemocyanin). It appeared that the presence of a carrier protein linked to chitosan was necessary to enhance the immune response and to obtain antibodies in a stable and reproducible way. Direct and inhibition enzyme‐linked immunosorbent assay experiments were performed to assess the affinity and the specificity of the antibodies. The interactions of these antibodies with modified chitosans showed no influence of the degree of polymerization of the polymer in the range studied (from 24 to 2261), by contrast with the degree of acetylation. The affinity decreased when the degree of acetylation increased. Absence of cross‐reactivity with glycosaminoglycans was observed whatever the antibody. The cationicity of the amine function along the polymer chains may have a role in the immunological recognition of the chitosan structure. © 2003 Wiley Periodicals, Inc. J Biomed Mater Res 67A: 766–774, 2003</description><subject>Acetylation</subject><subject>Animals</subject><subject>Antibodies - immunology</subject><subject>Antibodies - isolation & purification</subject><subject>Antibody Affinity</subject><subject>Antibody Formation</subject><subject>Antibody Specificity</subject><subject>Biological and medical sciences</subject><subject>Carrier Proteins</subject><subject>Chitin - analogs & derivatives</subject><subject>Chitin - immunology</subject><subject>Chitosan</subject><subject>Decapodiformes</subject><subject>degree of acetylation</subject><subject>ELISA</subject><subject>glycosaminoglycans</subject><subject>hemocyanin</subject><subject>Hemocyanins</subject><subject>Medical sciences</subject><subject>Molecular Weight</subject><subject>polyclonal antibodies</subject><subject>Protein Binding</subject><subject>Rabbits</subject><subject>Radiotherapy. Instrumental treatment. Physiotherapy. Reeducation. Rehabilitation, orthophony, crenotherapy. Diet therapy and various other treatments (general aspects)</subject><subject>Serum Albumin, Bovine</subject><subject>Technology. Biomaterials. Equipments. Material. Instrumentation</subject><issn>1549-3296</issn><issn>0021-9304</issn><issn>1552-4965</issn><issn>1097-4636</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0MtP3DAQB2ALFfEqJ-5oL-0FhWb8SnIsqy6vhVYqCKkXa-JMhCGPxc7y-O8x7LZ7KyePR9_MSD_G9iA9hDTl3-7K9hBjCYKvsS1Qiiey0OrTWy2LRPBCb7LtEO4i1qniG2wTpI6ayy2W_fI0Q4-D67sRdtWookdq-llL3TDq69gaXGJv3dAH7N5_ZV85Cp_Zeo1NoN3lu8OuJz-uxifJ9Ofx6fj7NLFKSJ7kkEvSStclpAVWWFKVl8DJcg5aWCqokDK3Kq2Ac04iUwRaZwqtyLIca7HDvi72znz_MKcwmNYFS02DHfXzYDIQhRRKfgihgExymUd4sIDW9yF4qs3Muxb9i4HUvAVqYqAGzXugUe8v187LlqqVXSYYwZclwGCxqT121oWVU4LnuRDRwcI9uYZe_nfTnB1d_D2eLGZcGOj53wz6e6OzmJW5uTw2R5M_cH5-Kcxv8Qp-MZtB</recordid><startdate>20031201</startdate><enddate>20031201</enddate><creator>Sorlier, Pierre</creator><creator>Hartmann, Daniel J.</creator><creator>Denuzière, Anne</creator><creator>Viton, Christophe</creator><creator>Domard, Alain</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><general>John Wiley & Sons</general><scope>BSCLL</scope><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>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20031201</creationdate><title>Preparation and development of anti-chitosan antibodies</title><author>Sorlier, Pierre ; Hartmann, Daniel J. ; Denuzière, Anne ; Viton, Christophe ; Domard, Alain</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5342-8184e656fb109adabed8b12ec22163ce9e9448c50d1222e375e16675ac3778af3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Acetylation</topic><topic>Animals</topic><topic>Antibodies - immunology</topic><topic>Antibodies - isolation & purification</topic><topic>Antibody Affinity</topic><topic>Antibody Formation</topic><topic>Antibody Specificity</topic><topic>Biological and medical sciences</topic><topic>Carrier Proteins</topic><topic>Chitin - analogs & derivatives</topic><topic>Chitin - immunology</topic><topic>Chitosan</topic><topic>Decapodiformes</topic><topic>degree of acetylation</topic><topic>ELISA</topic><topic>glycosaminoglycans</topic><topic>hemocyanin</topic><topic>Hemocyanins</topic><topic>Medical sciences</topic><topic>Molecular Weight</topic><topic>polyclonal antibodies</topic><topic>Protein Binding</topic><topic>Rabbits</topic><topic>Radiotherapy. Instrumental treatment. Physiotherapy. Reeducation. Rehabilitation, orthophony, crenotherapy. Diet therapy and various other treatments (general aspects)</topic><topic>Serum Albumin, Bovine</topic><topic>Technology. Biomaterials. Equipments. Material. Instrumentation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sorlier, Pierre</creatorcontrib><creatorcontrib>Hartmann, Daniel J.</creatorcontrib><creatorcontrib>Denuzière, Anne</creatorcontrib><creatorcontrib>Viton, Christophe</creatorcontrib><creatorcontrib>Domard, Alain</creatorcontrib><collection>Istex</collection><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>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of biomedical materials research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sorlier, Pierre</au><au>Hartmann, Daniel J.</au><au>Denuzière, Anne</au><au>Viton, Christophe</au><au>Domard, Alain</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Preparation and development of anti-chitosan antibodies</atitle><jtitle>Journal of biomedical materials research</jtitle><addtitle>J. Biomed. Mater. Res</addtitle><date>2003-12-01</date><risdate>2003</risdate><volume>67A</volume><issue>3</issue><spage>766</spage><epage>774</epage><pages>766-774</pages><issn>1549-3296</issn><issn>0021-9304</issn><eissn>1552-4965</eissn><eissn>1097-4636</eissn><coden>JBMRBG</coden><abstract>Polyclonal antibodies directed against chitosan were produced using several immunogens, prepared by binding the polymer according to two ways (covalent and electrostatic) with a protein (bovine serum albumin or hemocyanin). It appeared that the presence of a carrier protein linked to chitosan was necessary to enhance the immune response and to obtain antibodies in a stable and reproducible way. Direct and inhibition enzyme‐linked immunosorbent assay experiments were performed to assess the affinity and the specificity of the antibodies. The interactions of these antibodies with modified chitosans showed no influence of the degree of polymerization of the polymer in the range studied (from 24 to 2261), by contrast with the degree of acetylation. The affinity decreased when the degree of acetylation increased. Absence of cross‐reactivity with glycosaminoglycans was observed whatever the antibody. The cationicity of the amine function along the polymer chains may have a role in the immunological recognition of the chitosan structure. © 2003 Wiley Periodicals, Inc. J Biomed Mater Res 67A: 766–774, 2003</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>14613224</pmid><doi>10.1002/jbm.a.10132</doi><tpages>9</tpages></addata></record> |
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subjects | Acetylation Animals Antibodies - immunology Antibodies - isolation & purification Antibody Affinity Antibody Formation Antibody Specificity Biological and medical sciences Carrier Proteins Chitin - analogs & derivatives Chitin - immunology Chitosan Decapodiformes degree of acetylation ELISA glycosaminoglycans hemocyanin Hemocyanins Medical sciences Molecular Weight polyclonal antibodies Protein Binding Rabbits Radiotherapy. Instrumental treatment. Physiotherapy. Reeducation. Rehabilitation, orthophony, crenotherapy. Diet therapy and various other treatments (general aspects) Serum Albumin, Bovine Technology. Biomaterials. Equipments. Material. Instrumentation |
title | Preparation and development of anti-chitosan antibodies |
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