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
Hauptverfasser: Sorlier, Pierre, Hartmann, Daniel J., Denuzière, Anne, Viton, Christophe, Domard, Alain
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container_issue 3
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container_title Journal of biomedical materials research
container_volume 67A
creator Sorlier, Pierre
Hartmann, Daniel J.
Denuzière, Anne
Viton, Christophe
Domard, Alain
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 &amp; purification ; Antibody Affinity ; Antibody Formation ; Antibody Specificity ; Biological and medical sciences ; Carrier Proteins ; Chitin - analogs &amp; 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. 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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 &amp; 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 &amp; 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. 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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. 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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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source MEDLINE; Wiley Journals
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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