Large-scale preparation of thrombin from human plasma
Abstract Thrombin was prepared from human blood plasma (batch size 1200 L). First, prothrombin was isolated by the following separation techniques: cryoprecipitation, ion-exchange chromatography (diethyl aminoethyl, DEAE-IEX), heparin affinity chromatography, a second DEAE-IEX step, and immobilized...
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| Veröffentlicht in: | Thrombosis research 2008, Vol.122 (4), p.560-567 |
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| creator | Aizawa, Peter Winge, Stefan Karlsson, Göran |
| description | Abstract Thrombin was prepared from human blood plasma (batch size 1200 L). First, prothrombin was isolated by the following separation techniques: cryoprecipitation, ion-exchange chromatography (diethyl aminoethyl, DEAE-IEX), heparin affinity chromatography, a second DEAE-IEX step, and immobilized metal-affinity chromatography (IMAC). Prothrombin was then activated to thrombin, which was purified by hydrophobic interaction chromatography (HIC) and concentrated by ultrafiltration. This process is cost-effective because a waste fraction can be used from one of the steps (heparin affinity chromatography) in the commercial production of plasma-derived Factor IX (FIX). The final thrombin preparation had a purity of approximately 75% (specific activity approximately 2400 IU/mg protein), which is sufficient for its intended purpose in a fibrin glue. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), Factor X (FX) activity analysis, and analytical HIC were also used to characterize the thrombin. Three substantially different techniques were used to reduce any viral activity, namely: solvent/detergent (S/D) treatment, pasteurization, and virus filtration (nanofiltration). The manufacturing process presented here would be suitable for large-scale production of thrombin with a high degree of virus safety. |
| doi_str_mv | 10.1016/j.thromres.2007.12.027 |
| format | Article |
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First, prothrombin was isolated by the following separation techniques: cryoprecipitation, ion-exchange chromatography (diethyl aminoethyl, DEAE-IEX), heparin affinity chromatography, a second DEAE-IEX step, and immobilized metal-affinity chromatography (IMAC). Prothrombin was then activated to thrombin, which was purified by hydrophobic interaction chromatography (HIC) and concentrated by ultrafiltration. This process is cost-effective because a waste fraction can be used from one of the steps (heparin affinity chromatography) in the commercial production of plasma-derived Factor IX (FIX). The final thrombin preparation had a purity of approximately 75% (specific activity approximately 2400 IU/mg protein), which is sufficient for its intended purpose in a fibrin glue. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), Factor X (FX) activity analysis, and analytical HIC were also used to characterize the thrombin. Three substantially different techniques were used to reduce any viral activity, namely: solvent/detergent (S/D) treatment, pasteurization, and virus filtration (nanofiltration). The manufacturing process presented here would be suitable for large-scale production of thrombin with a high degree of virus safety.</description><identifier>ISSN: 0049-3848</identifier><identifier>EISSN: 1879-2472</identifier><identifier>DOI: 10.1016/j.thromres.2007.12.027</identifier><identifier>PMID: 18329699</identifier><identifier>CODEN: THBRAA</identifier><language>eng</language><publisher>New York, NY: Elsevier Ltd</publisher><subject>Biological and medical sciences ; Blood and lymphatic vessels ; Cardiology. Vascular system ; Chemistry, Clinical - methods ; Chromatography - methods ; Chromatography, Ion Exchange - methods ; Coronary heart disease ; Detergents - chemistry ; Detergents - pharmacology ; Diseases of the peripheral vessels. Diseases of the vena cava. Miscellaneous ; Electrophoresis, Polyacrylamide Gel ; Factor IX - chemistry ; Factor X - chemistry ; Fibrin glue ; Fibrin sealant ; Heart ; Hematology, Oncology and Palliative Medicine ; Heparin - chemistry ; Humans ; Ligands ; Medical sciences ; Prothrombin ; Prothrombin - chemistry ; Sepharose - chemistry ; Solvents - chemistry ; Thrombin ; Thrombin - biosynthesis ; Thrombin - chemistry ; Thrombin - isolation & purification ; Thrombin - metabolism ; Time Factors</subject><ispartof>Thrombosis research, 2008, Vol.122 (4), p.560-567</ispartof><rights>Elsevier Ltd</rights><rights>2008 Elsevier Ltd</rights><rights>2008 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c451t-b3c24078db526d0ef91eb8c0c8cf16c9783f246578c82a83a997b114fef569a13</citedby><cites>FETCH-LOGICAL-c451t-b3c24078db526d0ef91eb8c0c8cf16c9783f246578c82a83a997b114fef569a13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.thromres.2007.12.027$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,777,781,3537,4010,27904,27905,27906,45976</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=20598701$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18329699$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Aizawa, Peter</creatorcontrib><creatorcontrib>Winge, Stefan</creatorcontrib><creatorcontrib>Karlsson, Göran</creatorcontrib><title>Large-scale preparation of thrombin from human plasma</title><title>Thrombosis research</title><addtitle>Thromb Res</addtitle><description>Abstract Thrombin was prepared from human blood plasma (batch size 1200 L). First, prothrombin was isolated by the following separation techniques: cryoprecipitation, ion-exchange chromatography (diethyl aminoethyl, DEAE-IEX), heparin affinity chromatography, a second DEAE-IEX step, and immobilized metal-affinity chromatography (IMAC). Prothrombin was then activated to thrombin, which was purified by hydrophobic interaction chromatography (HIC) and concentrated by ultrafiltration. This process is cost-effective because a waste fraction can be used from one of the steps (heparin affinity chromatography) in the commercial production of plasma-derived Factor IX (FIX). The final thrombin preparation had a purity of approximately 75% (specific activity approximately 2400 IU/mg protein), which is sufficient for its intended purpose in a fibrin glue. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), Factor X (FX) activity analysis, and analytical HIC were also used to characterize the thrombin. Three substantially different techniques were used to reduce any viral activity, namely: solvent/detergent (S/D) treatment, pasteurization, and virus filtration (nanofiltration). The manufacturing process presented here would be suitable for large-scale production of thrombin with a high degree of virus safety.</description><subject>Biological and medical sciences</subject><subject>Blood and lymphatic vessels</subject><subject>Cardiology. Vascular system</subject><subject>Chemistry, Clinical - methods</subject><subject>Chromatography - methods</subject><subject>Chromatography, Ion Exchange - methods</subject><subject>Coronary heart disease</subject><subject>Detergents - chemistry</subject><subject>Detergents - pharmacology</subject><subject>Diseases of the peripheral vessels. Diseases of the vena cava. Miscellaneous</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Factor IX - chemistry</subject><subject>Factor X - chemistry</subject><subject>Fibrin glue</subject><subject>Fibrin sealant</subject><subject>Heart</subject><subject>Hematology, Oncology and Palliative Medicine</subject><subject>Heparin - chemistry</subject><subject>Humans</subject><subject>Ligands</subject><subject>Medical sciences</subject><subject>Prothrombin</subject><subject>Prothrombin - chemistry</subject><subject>Sepharose - chemistry</subject><subject>Solvents - chemistry</subject><subject>Thrombin</subject><subject>Thrombin - biosynthesis</subject><subject>Thrombin - chemistry</subject><subject>Thrombin - isolation & purification</subject><subject>Thrombin - metabolism</subject><subject>Time Factors</subject><issn>0049-3848</issn><issn>1879-2472</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1v1DAQhq0K1G4Lf6HKBW4JM86H7QsCVVCQVuJAe7YcZ0y95As7qdR_j8MuIHFhLnN5Zt7RM4xdIxQI2Lw5FMtDmIZAseAAokBeABdnbIdSqJxXgj9jO4BK5aWs5AW7jPEAgAJVfc4uUJZcNUrtWL034Rvl0ZqesjnQbIJZ_DRmk8t-JbR-zFzq2cM6mDGbexMH84I9d6aP9PLUr9j9xw93N5_y_Zfbzzfv97mtalzytrS8AiG7tuZNB-QUUistWGkdNlYJWTpeNbWQVnIjS6OUaBErR65ulMHyir0-7p3D9GOluOjBR0t9b0aa1qgbVUqBvE5gcwRtmGIM5PQc_GDCk0bQmzB90L-F6U2YRq6TsDR4fUpY24G6v2MnQwl4dQLMJskFM1of_3AcaiUFbKe-O3KUfDx6CjpaT6Olzgeyi-4m__9b3v6zwvZ-9Cn1Oz1RPExrGJNtjTqmAf11e-_2XZCQquLlT4y7oRg</recordid><startdate>2008</startdate><enddate>2008</enddate><creator>Aizawa, Peter</creator><creator>Winge, Stefan</creator><creator>Karlsson, Göran</creator><general>Elsevier Ltd</general><general>Elsevier Science</general><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></search><sort><creationdate>2008</creationdate><title>Large-scale preparation of thrombin from human plasma</title><author>Aizawa, Peter ; Winge, Stefan ; Karlsson, Göran</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c451t-b3c24078db526d0ef91eb8c0c8cf16c9783f246578c82a83a997b114fef569a13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Biological and medical sciences</topic><topic>Blood and lymphatic vessels</topic><topic>Cardiology. Vascular system</topic><topic>Chemistry, Clinical - methods</topic><topic>Chromatography - methods</topic><topic>Chromatography, Ion Exchange - methods</topic><topic>Coronary heart disease</topic><topic>Detergents - chemistry</topic><topic>Detergents - pharmacology</topic><topic>Diseases of the peripheral vessels. Diseases of the vena cava. Miscellaneous</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Factor IX - chemistry</topic><topic>Factor X - chemistry</topic><topic>Fibrin glue</topic><topic>Fibrin sealant</topic><topic>Heart</topic><topic>Hematology, Oncology and Palliative Medicine</topic><topic>Heparin - chemistry</topic><topic>Humans</topic><topic>Ligands</topic><topic>Medical sciences</topic><topic>Prothrombin</topic><topic>Prothrombin - chemistry</topic><topic>Sepharose - chemistry</topic><topic>Solvents - chemistry</topic><topic>Thrombin</topic><topic>Thrombin - biosynthesis</topic><topic>Thrombin - chemistry</topic><topic>Thrombin - isolation & purification</topic><topic>Thrombin - metabolism</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Aizawa, Peter</creatorcontrib><creatorcontrib>Winge, Stefan</creatorcontrib><creatorcontrib>Karlsson, Göran</creatorcontrib><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><jtitle>Thrombosis research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Aizawa, Peter</au><au>Winge, Stefan</au><au>Karlsson, Göran</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Large-scale preparation of thrombin from human plasma</atitle><jtitle>Thrombosis research</jtitle><addtitle>Thromb Res</addtitle><date>2008</date><risdate>2008</risdate><volume>122</volume><issue>4</issue><spage>560</spage><epage>567</epage><pages>560-567</pages><issn>0049-3848</issn><eissn>1879-2472</eissn><coden>THBRAA</coden><abstract>Abstract Thrombin was prepared from human blood plasma (batch size 1200 L). First, prothrombin was isolated by the following separation techniques: cryoprecipitation, ion-exchange chromatography (diethyl aminoethyl, DEAE-IEX), heparin affinity chromatography, a second DEAE-IEX step, and immobilized metal-affinity chromatography (IMAC). Prothrombin was then activated to thrombin, which was purified by hydrophobic interaction chromatography (HIC) and concentrated by ultrafiltration. This process is cost-effective because a waste fraction can be used from one of the steps (heparin affinity chromatography) in the commercial production of plasma-derived Factor IX (FIX). The final thrombin preparation had a purity of approximately 75% (specific activity approximately 2400 IU/mg protein), which is sufficient for its intended purpose in a fibrin glue. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), Factor X (FX) activity analysis, and analytical HIC were also used to characterize the thrombin. Three substantially different techniques were used to reduce any viral activity, namely: solvent/detergent (S/D) treatment, pasteurization, and virus filtration (nanofiltration). The manufacturing process presented here would be suitable for large-scale production of thrombin with a high degree of virus safety.</abstract><cop>New York, NY</cop><pub>Elsevier Ltd</pub><pmid>18329699</pmid><doi>10.1016/j.thromres.2007.12.027</doi><tpages>8</tpages></addata></record> |
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| subjects | Biological and medical sciences Blood and lymphatic vessels Cardiology. Vascular system Chemistry, Clinical - methods Chromatography - methods Chromatography, Ion Exchange - methods Coronary heart disease Detergents - chemistry Detergents - pharmacology Diseases of the peripheral vessels. Diseases of the vena cava. Miscellaneous Electrophoresis, Polyacrylamide Gel Factor IX - chemistry Factor X - chemistry Fibrin glue Fibrin sealant Heart Hematology, Oncology and Palliative Medicine Heparin - chemistry Humans Ligands Medical sciences Prothrombin Prothrombin - chemistry Sepharose - chemistry Solvents - chemistry Thrombin Thrombin - biosynthesis Thrombin - chemistry Thrombin - isolation & purification Thrombin - metabolism Time Factors |
| title | Large-scale preparation of thrombin from human plasma |
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