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Clots of beta-fibrin. Viscoelastic properties, temperature dependence of elasticity, and interaction with fibrinogen-binding tetrapeptides
Clots of human beta-fibrin, in which only (or predominantly) the B fibrinopeptide is released, were formed at 14 degrees C by copperhead venom procoagulant enzyme (CVE or venzyme), at pH 8.5, ionic strength 0.45. The shear modulus of elasticity increased slowly and after several days attained a cons...
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Published in: | Biophysical journal 1988-03, Vol.53 (3), p.311-318 |
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description | Clots of human beta-fibrin, in which only (or predominantly) the B fibrinopeptide is released, were formed at 14 degrees C by copperhead venom procoagulant enzyme (CVE or venzyme), at pH 8.5, ionic strength 0.45. The shear modulus of elasticity increased slowly and after several days attained a constant value, which was lower than those of alpha-fibrin or alpha beta-fibrin under the same conditions. Before studying the temperature dependence of elasticity, the CVE was then inhibited by introducing phenyl methyl sulfonyl chloride (PMSF) by diffusion. With increasing temperature, the modulus decreased progressively from 5 degrees C to nearly zero at 35 degrees and was essentially reversible with temperature change; recovery of elasticity after change from 34.5 degrees to 14 degrees required approximately 2 d but was considerably faster than the initial buildup of elasticity by CVE at 14 degrees. Creep and creep recovery measurements on unligated clots showed creep rates and irrecoverable deformation that were similar in magnitude to those of alpha-fibrin clots formed with batroxobin and much larger than those of alpha beta-fibrin clots formed with thrombin, under the same conditions. During creep and creep recovery, the differential modulus or compliance remained constant, showing that there was no permanent structural damage, and if network strands are severed in slow flow, they must rejoin in new configurations. |
doi_str_mv | 10.1016/S0006-3495(88)83108-4 |
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Viscoelastic properties, temperature dependence of elasticity, and interaction with fibrinogen-binding tetrapeptides</title><source>PubMed Central</source><creator>Shimizu, A. ; Ferry, J.D.</creator><creatorcontrib>Shimizu, A. ; Ferry, J.D.</creatorcontrib><description>Clots of human beta-fibrin, in which only (or predominantly) the B fibrinopeptide is released, were formed at 14 degrees C by copperhead venom procoagulant enzyme (CVE or venzyme), at pH 8.5, ionic strength 0.45. The shear modulus of elasticity increased slowly and after several days attained a constant value, which was lower than those of alpha-fibrin or alpha beta-fibrin under the same conditions. Before studying the temperature dependence of elasticity, the CVE was then inhibited by introducing phenyl methyl sulfonyl chloride (PMSF) by diffusion. With increasing temperature, the modulus decreased progressively from 5 degrees C to nearly zero at 35 degrees and was essentially reversible with temperature change; recovery of elasticity after change from 34.5 degrees to 14 degrees required approximately 2 d but was considerably faster than the initial buildup of elasticity by CVE at 14 degrees. Creep and creep recovery measurements on unligated clots showed creep rates and irrecoverable deformation that were similar in magnitude to those of alpha-fibrin clots formed with batroxobin and much larger than those of alpha beta-fibrin clots formed with thrombin, under the same conditions. During creep and creep recovery, the differential modulus or compliance remained constant, showing that there was no permanent structural damage, and if network strands are severed in slow flow, they must rejoin in new configurations.</description><identifier>ISSN: 0006-3495</identifier><identifier>EISSN: 1542-0086</identifier><identifier>DOI: 10.1016/S0006-3495(88)83108-4</identifier><identifier>PMID: 3349127</identifier><identifier>CODEN: BIOJAU</identifier><language>eng</language><publisher>Bethesda, MD: Elsevier Inc</publisher><subject>Biological and medical sciences ; Blood Coagulation ; Blood coagulation. Blood cells ; Elasticity ; Fibrin ; Fibrinogen ; Fibrinopeptide B ; Fundamental and applied biological sciences. Psychology ; General aspects, investigation methods, hemostasis, fibrinolysis ; Molecular and cellular biology ; Oligopeptides - metabolism ; Temperature ; Viscosity</subject><ispartof>Biophysical journal, 1988-03, Vol.53 (3), p.311-318</ispartof><rights>1988 The Biophysical Society</rights><rights>1989 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c491t-601ca25e0b2cf25da2779bc595bd34d07ed7749bf9c6bce644986f506512e6453</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1330199/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1330199/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27903,27904,53769,53771</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7060277$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3349127$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Shimizu, A.</creatorcontrib><creatorcontrib>Ferry, J.D.</creatorcontrib><title>Clots of beta-fibrin. Viscoelastic properties, temperature dependence of elasticity, and interaction with fibrinogen-binding tetrapeptides</title><title>Biophysical journal</title><addtitle>Biophys J</addtitle><description>Clots of human beta-fibrin, in which only (or predominantly) the B fibrinopeptide is released, were formed at 14 degrees C by copperhead venom procoagulant enzyme (CVE or venzyme), at pH 8.5, ionic strength 0.45. The shear modulus of elasticity increased slowly and after several days attained a constant value, which was lower than those of alpha-fibrin or alpha beta-fibrin under the same conditions. Before studying the temperature dependence of elasticity, the CVE was then inhibited by introducing phenyl methyl sulfonyl chloride (PMSF) by diffusion. With increasing temperature, the modulus decreased progressively from 5 degrees C to nearly zero at 35 degrees and was essentially reversible with temperature change; recovery of elasticity after change from 34.5 degrees to 14 degrees required approximately 2 d but was considerably faster than the initial buildup of elasticity by CVE at 14 degrees. Creep and creep recovery measurements on unligated clots showed creep rates and irrecoverable deformation that were similar in magnitude to those of alpha-fibrin clots formed with batroxobin and much larger than those of alpha beta-fibrin clots formed with thrombin, under the same conditions. During creep and creep recovery, the differential modulus or compliance remained constant, showing that there was no permanent structural damage, and if network strands are severed in slow flow, they must rejoin in new configurations.</description><subject>Biological and medical sciences</subject><subject>Blood Coagulation</subject><subject>Blood coagulation. Blood cells</subject><subject>Elasticity</subject><subject>Fibrin</subject><subject>Fibrinogen</subject><subject>Fibrinopeptide B</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>General aspects, investigation methods, hemostasis, fibrinolysis</subject><subject>Molecular and cellular biology</subject><subject>Oligopeptides - metabolism</subject><subject>Temperature</subject><subject>Viscosity</subject><issn>0006-3495</issn><issn>1542-0086</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><recordid>eNqFkd1u1DAQhS0EKkvhESr5AiEqNcVO4sS5KUIroJUqccHPreXYk-2grB1sb1FfoU-N041W5apX_plvzhzNIeSEs3POePPhO2OsKaq6E--lPJUVZ7Kon5EVF3VZMCab52R1QF6SVzH-ZoyXgvEjclTlT162K3K_Hn2K1A-0h6SLAfuA7pz-wmg8jDomNHQKfoKQEOIZTbDNd512AaiFCZwFZ2DuX2hMd2dUO0vRpQyahN7Rv5hu6F7bb8AVPTqLbpPVUtATTAktxNfkxaDHCG-W85j8_PL5x_qyuP729Wr96bow2XMqGsaNLgWwvjRDKawu27brjehEb6vashZs29ZdP3Sm6Q00dd3JZhCsEbzML1Edk4u97rTrt2ANuGxiVFPArQ53ymtU_1cc3qiNv1W8qhjvuizwbhEI_s8OYlLbvC4YR-3A76JqZSaFnCeJPWiCjzHAcBjCmZpDVA8hqjkhJaV6CFHVue_kscND15Jarr9d6joaPQ5BO4PxgLWsYXkpGfu4xyBv8xYhqGhwjstiAJOU9fiEkX-UOb1o</recordid><startdate>19880301</startdate><enddate>19880301</enddate><creator>Shimizu, A.</creator><creator>Ferry, J.D.</creator><general>Elsevier Inc</general><general>Biophysical Society</general><general>The Biophysical Society</general><scope>6I.</scope><scope>AAFTH</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>7X8</scope><scope>5PM</scope></search><sort><creationdate>19880301</creationdate><title>Clots of beta-fibrin. Viscoelastic properties, temperature dependence of elasticity, and interaction with fibrinogen-binding tetrapeptides</title><author>Shimizu, A. ; Ferry, J.D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c491t-601ca25e0b2cf25da2779bc595bd34d07ed7749bf9c6bce644986f506512e6453</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>Biological and medical sciences</topic><topic>Blood Coagulation</topic><topic>Blood coagulation. Blood cells</topic><topic>Elasticity</topic><topic>Fibrin</topic><topic>Fibrinogen</topic><topic>Fibrinopeptide B</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>General aspects, investigation methods, hemostasis, fibrinolysis</topic><topic>Molecular and cellular biology</topic><topic>Oligopeptides - metabolism</topic><topic>Temperature</topic><topic>Viscosity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shimizu, A.</creatorcontrib><creatorcontrib>Ferry, J.D.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biophysical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shimizu, A.</au><au>Ferry, J.D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Clots of beta-fibrin. Viscoelastic properties, temperature dependence of elasticity, and interaction with fibrinogen-binding tetrapeptides</atitle><jtitle>Biophysical journal</jtitle><addtitle>Biophys J</addtitle><date>1988-03-01</date><risdate>1988</risdate><volume>53</volume><issue>3</issue><spage>311</spage><epage>318</epage><pages>311-318</pages><issn>0006-3495</issn><eissn>1542-0086</eissn><coden>BIOJAU</coden><abstract>Clots of human beta-fibrin, in which only (or predominantly) the B fibrinopeptide is released, were formed at 14 degrees C by copperhead venom procoagulant enzyme (CVE or venzyme), at pH 8.5, ionic strength 0.45. The shear modulus of elasticity increased slowly and after several days attained a constant value, which was lower than those of alpha-fibrin or alpha beta-fibrin under the same conditions. Before studying the temperature dependence of elasticity, the CVE was then inhibited by introducing phenyl methyl sulfonyl chloride (PMSF) by diffusion. With increasing temperature, the modulus decreased progressively from 5 degrees C to nearly zero at 35 degrees and was essentially reversible with temperature change; recovery of elasticity after change from 34.5 degrees to 14 degrees required approximately 2 d but was considerably faster than the initial buildup of elasticity by CVE at 14 degrees. Creep and creep recovery measurements on unligated clots showed creep rates and irrecoverable deformation that were similar in magnitude to those of alpha-fibrin clots formed with batroxobin and much larger than those of alpha beta-fibrin clots formed with thrombin, under the same conditions. During creep and creep recovery, the differential modulus or compliance remained constant, showing that there was no permanent structural damage, and if network strands are severed in slow flow, they must rejoin in new configurations.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>3349127</pmid><doi>10.1016/S0006-3495(88)83108-4</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Biological and medical sciences Blood Coagulation Blood coagulation. Blood cells Elasticity Fibrin Fibrinogen Fibrinopeptide B Fundamental and applied biological sciences. Psychology General aspects, investigation methods, hemostasis, fibrinolysis Molecular and cellular biology Oligopeptides - metabolism Temperature Viscosity |
title | Clots of beta-fibrin. Viscoelastic properties, temperature dependence of elasticity, and interaction with fibrinogen-binding tetrapeptides |
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