Rheological characterization and dissolution kinetics of fibrin gels crosslinked by a microbial transglutaminase
Various fibrin gels were prepared with a microbial transglutaminase under miscellaneous conditions. The gels were characterized through their rheological properties. The influence of fibronectin addition and that of covalent bonding on the viscoelastic characteristics were evaluated. Gel elasticity...
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Veröffentlicht in: | Biopolymers 2005-04, Vol.77 (5), p.257-263 |
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creator | Sun, Yan Giraudier, Olivier Garde, Véronique Larreta |
description | Various fibrin gels were prepared with a microbial transglutaminase under miscellaneous conditions. The gels were characterized through their rheological properties. The influence of fibronectin addition and that of covalent bonding on the viscoelastic characteristics were evaluated. Gel elasticity is proportional to fibrinogen concentration but shows a nonlinear dependence on transglutaminase concentration. Additional crosslink of fibronectin in fibrin gels has no effect on the rheological character of the matrix. Dissolution kinetics in concentrated urea solutions evidences the role of covalent bonds on gel stability. The rheological properties and gel stability are discussed in relation with the enzyme‐catalyzed covalent bonding. The microbial enzyme reactions are compared to those of FXIII and tissue transglutaminases. © 2005 Wiley Periodicals, Inc. Biopolymers, 2005 |
doi_str_mv | 10.1002/bip.20177 |
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The gels were characterized through their rheological properties. The influence of fibronectin addition and that of covalent bonding on the viscoelastic characteristics were evaluated. Gel elasticity is proportional to fibrinogen concentration but shows a nonlinear dependence on transglutaminase concentration. Additional crosslink of fibronectin in fibrin gels has no effect on the rheological character of the matrix. Dissolution kinetics in concentrated urea solutions evidences the role of covalent bonds on gel stability. The rheological properties and gel stability are discussed in relation with the enzyme‐catalyzed covalent bonding. The microbial enzyme reactions are compared to those of FXIII and tissue transglutaminases. © 2005 Wiley Periodicals, Inc. Biopolymers, 2005</description><identifier>ISSN: 0006-3525</identifier><identifier>EISSN: 1097-0282</identifier><identifier>DOI: 10.1002/bip.20177</identifier><identifier>PMID: 15700298</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Cross-Linking Reagents - metabolism ; fibrin ; Fibrin - chemistry ; Fibrin - metabolism ; fibronectin ; Fibronectins - chemistry ; gels ; Gels - chemistry ; Gels - metabolism ; Kinetics ; microbial transglutaminase ; Rheology ; Transglutaminases - metabolism</subject><ispartof>Biopolymers, 2005-04, Vol.77 (5), p.257-263</ispartof><rights>Copyright © 2005 Wiley Periodicals, Inc.</rights><rights>Copyright (c) 2005 Wiley Periodicals, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3927-a40d4ae8e44b446138f1aacd2bef650ea7d4b257a246daeeba09d556cf1014dd3</citedby><cites>FETCH-LOGICAL-c3927-a40d4ae8e44b446138f1aacd2bef650ea7d4b257a246daeeba09d556cf1014dd3</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%2Fbip.20177$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fbip.20177$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27923,27924,45573,45574</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15700298$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sun, Yan</creatorcontrib><creatorcontrib>Giraudier, Olivier</creatorcontrib><creatorcontrib>Garde, Véronique Larreta</creatorcontrib><title>Rheological characterization and dissolution kinetics of fibrin gels crosslinked by a microbial transglutaminase</title><title>Biopolymers</title><addtitle>Biopolymers</addtitle><description>Various fibrin gels were prepared with a microbial transglutaminase under miscellaneous conditions. The gels were characterized through their rheological properties. The influence of fibronectin addition and that of covalent bonding on the viscoelastic characteristics were evaluated. Gel elasticity is proportional to fibrinogen concentration but shows a nonlinear dependence on transglutaminase concentration. Additional crosslink of fibronectin in fibrin gels has no effect on the rheological character of the matrix. Dissolution kinetics in concentrated urea solutions evidences the role of covalent bonds on gel stability. The rheological properties and gel stability are discussed in relation with the enzyme‐catalyzed covalent bonding. The microbial enzyme reactions are compared to those of FXIII and tissue transglutaminases. © 2005 Wiley Periodicals, Inc. Biopolymers, 2005</description><subject>Cross-Linking Reagents - metabolism</subject><subject>fibrin</subject><subject>Fibrin - chemistry</subject><subject>Fibrin - metabolism</subject><subject>fibronectin</subject><subject>Fibronectins - chemistry</subject><subject>gels</subject><subject>Gels - chemistry</subject><subject>Gels - metabolism</subject><subject>Kinetics</subject><subject>microbial transglutaminase</subject><subject>Rheology</subject><subject>Transglutaminases - metabolism</subject><issn>0006-3525</issn><issn>1097-0282</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUFvFCEYhonR2G314B8wnEw8TAsDDDNHXW1t0mhjNB7JB3yzxWVmVpiNbn-9uLvqyXgikOd9yPe9hDzj7JwzVl_YsDmvGdf6AVlw1umK1W39kCwYY00lVK1OyGnOXxmTUnD2mJxwpUuuaxdk8_EOpzitgoNI3R0kcDOmcA9zmEYKo6c-5DzF7f6-DiPOwWU69bQPNoWRrjBm6tKUcwzjGj21Owp0COXJhuKcE4x5VfIwhBEyPiGPeogZnx7PM_L58u2n5bvq5sPV9fLVTeVEV-sKJPMSsEUprZQNF23PAZyvLfaNYgjaS1srDbVsPCBaYJ1XqnE9Z1x6L87Ii4N3k6ZvW8yzGUJ2GCOMOG2zabTiQqr2vyDXSjCtuwK-PID7aRP2ZpPCAGlnODO_ejClB7PvobDPj9KtHdD_JY-LL8DFAfgeIu7-bTKvr29_K6tDIuQZf_xJQFqXWYRW5sv7K6OXb27LH5emEz8BW7ijvw</recordid><startdate>20050405</startdate><enddate>20050405</enddate><creator>Sun, Yan</creator><creator>Giraudier, Olivier</creator><creator>Garde, Véronique Larreta</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><scope>BSCLL</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>20050405</creationdate><title>Rheological characterization and dissolution kinetics of fibrin gels crosslinked by a microbial transglutaminase</title><author>Sun, Yan ; Giraudier, Olivier ; Garde, Véronique Larreta</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3927-a40d4ae8e44b446138f1aacd2bef650ea7d4b257a246daeeba09d556cf1014dd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Cross-Linking Reagents - metabolism</topic><topic>fibrin</topic><topic>Fibrin - chemistry</topic><topic>Fibrin - metabolism</topic><topic>fibronectin</topic><topic>Fibronectins - chemistry</topic><topic>gels</topic><topic>Gels - chemistry</topic><topic>Gels - metabolism</topic><topic>Kinetics</topic><topic>microbial transglutaminase</topic><topic>Rheology</topic><topic>Transglutaminases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sun, Yan</creatorcontrib><creatorcontrib>Giraudier, Olivier</creatorcontrib><creatorcontrib>Garde, Véronique Larreta</creatorcontrib><collection>Istex</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>Biopolymers</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sun, Yan</au><au>Giraudier, Olivier</au><au>Garde, Véronique Larreta</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Rheological characterization and dissolution kinetics of fibrin gels crosslinked by a microbial transglutaminase</atitle><jtitle>Biopolymers</jtitle><addtitle>Biopolymers</addtitle><date>2005-04-05</date><risdate>2005</risdate><volume>77</volume><issue>5</issue><spage>257</spage><epage>263</epage><pages>257-263</pages><issn>0006-3525</issn><eissn>1097-0282</eissn><abstract>Various fibrin gels were prepared with a microbial transglutaminase under miscellaneous conditions. The gels were characterized through their rheological properties. The influence of fibronectin addition and that of covalent bonding on the viscoelastic characteristics were evaluated. Gel elasticity is proportional to fibrinogen concentration but shows a nonlinear dependence on transglutaminase concentration. Additional crosslink of fibronectin in fibrin gels has no effect on the rheological character of the matrix. Dissolution kinetics in concentrated urea solutions evidences the role of covalent bonds on gel stability. The rheological properties and gel stability are discussed in relation with the enzyme‐catalyzed covalent bonding. The microbial enzyme reactions are compared to those of FXIII and tissue transglutaminases. © 2005 Wiley Periodicals, Inc. Biopolymers, 2005</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>15700298</pmid><doi>10.1002/bip.20177</doi><tpages>7</tpages></addata></record> |
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subjects | Cross-Linking Reagents - metabolism fibrin Fibrin - chemistry Fibrin - metabolism fibronectin Fibronectins - chemistry gels Gels - chemistry Gels - metabolism Kinetics microbial transglutaminase Rheology Transglutaminases - metabolism |
title | Rheological characterization and dissolution kinetics of fibrin gels crosslinked by a microbial transglutaminase |
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