[17] Meizothrombin: Active intermediate formed during prothrombinase-catalyzed activation of prothrombin
This chapter focuses on the active intermediate formed during the prothrombinase-catalyzed activation of prothrombin. The activation of prothrombin to thrombin proceeds via the cleavage of two peptide bonds in the prothrombin molecule. These bonds are cleaved by the prothrombinase enzyme complex tha...
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| Veröffentlicht in: | Methods in Enzymology 1993, Vol.222, p.299-312 |
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| creator | Doyle, Margaret F. Haley, Paul E. |
| description | This chapter focuses on the active intermediate formed during the prothrombinase-catalyzed activation of prothrombin. The activation of prothrombin to thrombin proceeds via the cleavage of two peptide bonds in the prothrombin molecule. These bonds are cleaved by the prothrombinase enzyme complex that is composed of the enzyme, factor Xa, and a cofactor, factor Va, assembled on a phospholipid surface in the presence of calcium ions. Further studies on the activation of human prothrombin indicate that the formation of meizothrombin as an intermediate is a consequence of the association of the cofactor, human factor Va, with the enzyme, human factor Xa, on the phospholipid surface. The absence of factor Va causes the activation to proceed via the prethrombin-2 intermediate. The observation that meizothrombin binds dansylarginine-N-(3-ethyl-l,5-pentanediyl)amide (DAPA) indicates that the intermediate has expressed an active site, and therefore could possibly have activity similar to thrombin. To determine the activity of meizothrombin, it first becomes necessary to obtain the intermediate in a stable form suitable for study. |
| doi_str_mv | 10.1016/0076-6879(93)22020-G |
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The activation of prothrombin to thrombin proceeds via the cleavage of two peptide bonds in the prothrombin molecule. These bonds are cleaved by the prothrombinase enzyme complex that is composed of the enzyme, factor Xa, and a cofactor, factor Va, assembled on a phospholipid surface in the presence of calcium ions. Further studies on the activation of human prothrombin indicate that the formation of meizothrombin as an intermediate is a consequence of the association of the cofactor, human factor Va, with the enzyme, human factor Xa, on the phospholipid surface. The absence of factor Va causes the activation to proceed via the prethrombin-2 intermediate. The observation that meizothrombin binds dansylarginine-N-(3-ethyl-l,5-pentanediyl)amide (DAPA) indicates that the intermediate has expressed an active site, and therefore could possibly have activity similar to thrombin. To determine the activity of meizothrombin, it first becomes necessary to obtain the intermediate in a stable form suitable for study.</description><identifier>ISSN: 0076-6879</identifier><identifier>ISBN: 9780121821234</identifier><identifier>ISBN: 0121821234</identifier><identifier>EISSN: 1557-7988</identifier><identifier>DOI: 10.1016/0076-6879(93)22020-G</identifier><identifier>PMID: 8412800</identifier><language>eng</language><publisher>United States: Elsevier Science & Technology</publisher><subject>Animals ; Binding Sites ; Blood Coagulation Tests - methods ; Electrophoresis, Polyacrylamide Gel - methods ; Enzyme Precursors - analysis ; Enzyme Precursors - metabolism ; Enzyme Precursors - pharmacology ; Esterases - metabolism ; Factor V - metabolism ; Factor Va - metabolism ; Femoral Artery - drug effects ; Femoral Artery - physiology ; Humans ; In Vitro Techniques ; Indicators and Reagents ; Kinetics ; Male ; Models, Biological ; Muscle Contraction - drug effects ; Muscle, Smooth, Vascular - drug effects ; Muscle, Smooth, Vascular - physiology ; Platelet Activation - drug effects ; Platelet Aggregation - drug effects ; Protein C - metabolism ; Prothrombin - metabolism ; Rabbits ; Spectrophotometry - methods ; Substrate Specificity ; Thrombin - analysis ; Thrombin - metabolism ; Thrombin - pharmacology ; Thromboplastin - metabolism</subject><ispartof>Methods in Enzymology, 1993, Vol.222, p.299-312</ispartof><rights>1993</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c312t-8b699eed7efe4b6ba1c5b022338cbe8903a40b5c5b4a9d44c73d3d9c79fa13eb3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/007668799322020G$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,775,776,780,789,3446,3537,4010,11267,27900,27901,27902,45786,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8412800$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Doyle, Margaret F.</creatorcontrib><creatorcontrib>Haley, Paul E.</creatorcontrib><title>[17] Meizothrombin: Active intermediate formed during prothrombinase-catalyzed activation of prothrombin</title><title>Methods in Enzymology</title><addtitle>Methods Enzymol</addtitle><description>This chapter focuses on the active intermediate formed during the prothrombinase-catalyzed activation of prothrombin. The activation of prothrombin to thrombin proceeds via the cleavage of two peptide bonds in the prothrombin molecule. These bonds are cleaved by the prothrombinase enzyme complex that is composed of the enzyme, factor Xa, and a cofactor, factor Va, assembled on a phospholipid surface in the presence of calcium ions. Further studies on the activation of human prothrombin indicate that the formation of meizothrombin as an intermediate is a consequence of the association of the cofactor, human factor Va, with the enzyme, human factor Xa, on the phospholipid surface. The absence of factor Va causes the activation to proceed via the prethrombin-2 intermediate. The observation that meizothrombin binds dansylarginine-N-(3-ethyl-l,5-pentanediyl)amide (DAPA) indicates that the intermediate has expressed an active site, and therefore could possibly have activity similar to thrombin. To determine the activity of meizothrombin, it first becomes necessary to obtain the intermediate in a stable form suitable for study.</description><subject>Animals</subject><subject>Binding Sites</subject><subject>Blood Coagulation Tests - methods</subject><subject>Electrophoresis, Polyacrylamide Gel - methods</subject><subject>Enzyme Precursors - analysis</subject><subject>Enzyme Precursors - metabolism</subject><subject>Enzyme Precursors - pharmacology</subject><subject>Esterases - metabolism</subject><subject>Factor V - metabolism</subject><subject>Factor Va - metabolism</subject><subject>Femoral Artery - drug effects</subject><subject>Femoral Artery - physiology</subject><subject>Humans</subject><subject>In Vitro Techniques</subject><subject>Indicators and Reagents</subject><subject>Kinetics</subject><subject>Male</subject><subject>Models, Biological</subject><subject>Muscle Contraction - drug effects</subject><subject>Muscle, Smooth, Vascular - drug effects</subject><subject>Muscle, Smooth, Vascular - physiology</subject><subject>Platelet Activation - drug effects</subject><subject>Platelet Aggregation - drug effects</subject><subject>Protein C - metabolism</subject><subject>Prothrombin - metabolism</subject><subject>Rabbits</subject><subject>Spectrophotometry - methods</subject><subject>Substrate Specificity</subject><subject>Thrombin - analysis</subject><subject>Thrombin - metabolism</subject><subject>Thrombin - pharmacology</subject><subject>Thromboplastin - metabolism</subject><issn>0076-6879</issn><issn>1557-7988</issn><isbn>9780121821234</isbn><isbn>0121821234</isbn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpNUUtLw0AQXnxQi_YfKOQkeojuI8nuehBK0SpUvOhJZNndTOxKmtRkU2h_vRtbinOZYb5vXt8gdE7wDcEku8WYZ3EmuLyS7JpSTHE8PUBDkqY85lKIQzSSXGBCiaCEsuQIDfclJ2jUtt84WCJpxvkADURCqMB4iOYfhH9GL-A2tZ839cK46i4aW-9WELnKQ7OA3GkPUVH3YZR3jau-omWzp-sWYqu9LtebgOu-VHtXV1Fd_KedoeNCly2Mdv4UvT8-vE2e4tnr9HkynsWWEepjYTIpAXIOBSQmM5rY1GBKGRPWgJCY6QSbNCQTLfMksZzlLJeWy0ITBoadostt3zD7p4PWq4VrLZSlrqDuWsUzjInkWSBe7IidCZepZeMWulmrnTQBv9_iELZdOWhUax1UNujRgPUqr50iWPXfUb3UqpdaSab-vqOm7BedI4Ci</recordid><startdate>1993</startdate><enddate>1993</enddate><creator>Doyle, Margaret F.</creator><creator>Haley, Paul E.</creator><general>Elsevier Science & Technology</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>1993</creationdate><title>[17] Meizothrombin: Active intermediate formed during prothrombinase-catalyzed activation of prothrombin</title><author>Doyle, Margaret F. ; Haley, Paul E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c312t-8b699eed7efe4b6ba1c5b022338cbe8903a40b5c5b4a9d44c73d3d9c79fa13eb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Animals</topic><topic>Binding Sites</topic><topic>Blood Coagulation Tests - methods</topic><topic>Electrophoresis, Polyacrylamide Gel - methods</topic><topic>Enzyme Precursors - analysis</topic><topic>Enzyme Precursors - metabolism</topic><topic>Enzyme Precursors - pharmacology</topic><topic>Esterases - metabolism</topic><topic>Factor V - metabolism</topic><topic>Factor Va - metabolism</topic><topic>Femoral Artery - drug effects</topic><topic>Femoral Artery - physiology</topic><topic>Humans</topic><topic>In Vitro Techniques</topic><topic>Indicators and Reagents</topic><topic>Kinetics</topic><topic>Male</topic><topic>Models, Biological</topic><topic>Muscle Contraction - drug effects</topic><topic>Muscle, Smooth, Vascular - drug effects</topic><topic>Muscle, Smooth, Vascular - physiology</topic><topic>Platelet Activation - drug effects</topic><topic>Platelet Aggregation - drug effects</topic><topic>Protein C - metabolism</topic><topic>Prothrombin - metabolism</topic><topic>Rabbits</topic><topic>Spectrophotometry - methods</topic><topic>Substrate Specificity</topic><topic>Thrombin - analysis</topic><topic>Thrombin - metabolism</topic><topic>Thrombin - pharmacology</topic><topic>Thromboplastin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Doyle, Margaret F.</creatorcontrib><creatorcontrib>Haley, Paul E.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Methods in Enzymology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Doyle, Margaret F.</au><au>Haley, Paul E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>[17] Meizothrombin: Active intermediate formed during prothrombinase-catalyzed activation of prothrombin</atitle><jtitle>Methods in Enzymology</jtitle><addtitle>Methods Enzymol</addtitle><date>1993</date><risdate>1993</risdate><volume>222</volume><spage>299</spage><epage>312</epage><pages>299-312</pages><issn>0076-6879</issn><eissn>1557-7988</eissn><isbn>9780121821234</isbn><isbn>0121821234</isbn><abstract>This chapter focuses on the active intermediate formed during the prothrombinase-catalyzed activation of prothrombin. The activation of prothrombin to thrombin proceeds via the cleavage of two peptide bonds in the prothrombin molecule. These bonds are cleaved by the prothrombinase enzyme complex that is composed of the enzyme, factor Xa, and a cofactor, factor Va, assembled on a phospholipid surface in the presence of calcium ions. Further studies on the activation of human prothrombin indicate that the formation of meizothrombin as an intermediate is a consequence of the association of the cofactor, human factor Va, with the enzyme, human factor Xa, on the phospholipid surface. The absence of factor Va causes the activation to proceed via the prethrombin-2 intermediate. The observation that meizothrombin binds dansylarginine-N-(3-ethyl-l,5-pentanediyl)amide (DAPA) indicates that the intermediate has expressed an active site, and therefore could possibly have activity similar to thrombin. To determine the activity of meizothrombin, it first becomes necessary to obtain the intermediate in a stable form suitable for study.</abstract><cop>United States</cop><pub>Elsevier Science & Technology</pub><pmid>8412800</pmid><doi>10.1016/0076-6879(93)22020-G</doi><tpages>14</tpages></addata></record> |
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| subjects | Animals Binding Sites Blood Coagulation Tests - methods Electrophoresis, Polyacrylamide Gel - methods Enzyme Precursors - analysis Enzyme Precursors - metabolism Enzyme Precursors - pharmacology Esterases - metabolism Factor V - metabolism Factor Va - metabolism Femoral Artery - drug effects Femoral Artery - physiology Humans In Vitro Techniques Indicators and Reagents Kinetics Male Models, Biological Muscle Contraction - drug effects Muscle, Smooth, Vascular - drug effects Muscle, Smooth, Vascular - physiology Platelet Activation - drug effects Platelet Aggregation - drug effects Protein C - metabolism Prothrombin - metabolism Rabbits Spectrophotometry - methods Substrate Specificity Thrombin - analysis Thrombin - metabolism Thrombin - pharmacology Thromboplastin - metabolism |
| title | [17] Meizothrombin: Active intermediate formed during prothrombinase-catalyzed activation of prothrombin |
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