Choline inhibition of prothrombin activation
A computer-interfaced spectrophotometric kinetic assay for prothrombin activation was developed, coupling the production of thrombin to a thrombin-specific amidolytic chromogenic reaction. As thrombin accumulated initially at constant velocity, the simultaneous release from S-2238 of pNA conformed t...
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| Veröffentlicht in: | Thrombosis research 1991-06, Vol.62 (6), p.635-648 |
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| container_title | Thrombosis research |
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| creator | Leach, Richard D. Dewind, Sally A. Slattery, Charles W. Herrmann, E.Clifford |
| description | A computer-interfaced spectrophotometric kinetic assay for prothrombin activation was developed, coupling the production of thrombin to a thrombin-specific amidolytic chromogenic reaction. As thrombin accumulated initially at constant velocity, the simultaneous release from S-2238 of pNA conformed to an acceleration function. Adherence to the acceleration function of the temporally increasing
A
400 of pNA was evaluated after transforming the data into linear format which permitted linear regression analysis. High correlation coefficients, routinely >0.99, verified linearity of thrombin production in individual assay mixtures. As prothrombin concentrations were varied, factor Xa exhibited Michaelis-Menten kinetics. Added choline produced a pattern of mixed-type inhibition. Replots of LB slopes and intercepts versus choline concentration gave apparent
K
i
and
K
i
values (mM): 22±3 and 48±7 without factor Va, 25±4 and 41±4 with factor Va. |
| doi_str_mv | 10.1016/0049-3848(91)90368-7 |
| format | Article |
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A
400 of pNA was evaluated after transforming the data into linear format which permitted linear regression analysis. High correlation coefficients, routinely >0.99, verified linearity of thrombin production in individual assay mixtures. As prothrombin concentrations were varied, factor Xa exhibited Michaelis-Menten kinetics. Added choline produced a pattern of mixed-type inhibition. Replots of LB slopes and intercepts versus choline concentration gave apparent
K
i
and
K
i
values (mM): 22±3 and 48±7 without factor Va, 25±4 and 41±4 with factor Va.</description><identifier>ISSN: 0049-3848</identifier><identifier>EISSN: 1879-2472</identifier><identifier>DOI: 10.1016/0049-3848(91)90368-7</identifier><identifier>PMID: 1926057</identifier><identifier>CODEN: THBRAA</identifier><language>eng</language><publisher>New York, NY: Elsevier Ltd</publisher><subject>anticoagulant ; Aspirin - pharmacology ; Biological and medical sciences ; Blood coagulation. Blood cells ; Calcium - pharmacology ; choline ; Choline - pharmacology ; chromogenic peptide substrate ; Coagulation factors ; Dipeptides - pharmacology ; Enzyme Activation - drug effects ; enzyme inhibitor ; factor Va ; Factor Xa Inhibitors ; Fundamental and applied biological sciences. Psychology ; Humans ; Kinetics ; Liposomes ; Microcomputers ; Molecular and cellular biology ; Phospholipids - pharmacology ; Prothrombin - metabolism ; prothrombinase ; Spectrophotometry ; Thromboplastin - antagonists & inhibitors</subject><ispartof>Thrombosis research, 1991-06, Vol.62 (6), p.635-648</ispartof><rights>1991</rights><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c386t-27152434127bf18fe5052f9a052ea0d01f29baf070b580b3fc90604955933e7e3</citedby><cites>FETCH-LOGICAL-c386t-27152434127bf18fe5052f9a052ea0d01f29baf070b580b3fc90604955933e7e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0049-3848(91)90368-7$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4966450$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1926057$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Leach, Richard D.</creatorcontrib><creatorcontrib>Dewind, Sally A.</creatorcontrib><creatorcontrib>Slattery, Charles W.</creatorcontrib><creatorcontrib>Herrmann, E.Clifford</creatorcontrib><title>Choline inhibition of prothrombin activation</title><title>Thrombosis research</title><addtitle>Thromb Res</addtitle><description>A computer-interfaced spectrophotometric kinetic assay for prothrombin activation was developed, coupling the production of thrombin to a thrombin-specific amidolytic chromogenic reaction. As thrombin accumulated initially at constant velocity, the simultaneous release from S-2238 of pNA conformed to an acceleration function. Adherence to the acceleration function of the temporally increasing
A
400 of pNA was evaluated after transforming the data into linear format which permitted linear regression analysis. High correlation coefficients, routinely >0.99, verified linearity of thrombin production in individual assay mixtures. As prothrombin concentrations were varied, factor Xa exhibited Michaelis-Menten kinetics. Added choline produced a pattern of mixed-type inhibition. Replots of LB slopes and intercepts versus choline concentration gave apparent
K
i
and
K
i
values (mM): 22±3 and 48±7 without factor Va, 25±4 and 41±4 with factor Va.</description><subject>anticoagulant</subject><subject>Aspirin - pharmacology</subject><subject>Biological and medical sciences</subject><subject>Blood coagulation. Blood cells</subject><subject>Calcium - pharmacology</subject><subject>choline</subject><subject>Choline - pharmacology</subject><subject>chromogenic peptide substrate</subject><subject>Coagulation factors</subject><subject>Dipeptides - pharmacology</subject><subject>Enzyme Activation - drug effects</subject><subject>enzyme inhibitor</subject><subject>factor Va</subject><subject>Factor Xa Inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Kinetics</subject><subject>Liposomes</subject><subject>Microcomputers</subject><subject>Molecular and cellular biology</subject><subject>Phospholipids - pharmacology</subject><subject>Prothrombin - metabolism</subject><subject>prothrombinase</subject><subject>Spectrophotometry</subject><subject>Thromboplastin - antagonists & inhibitors</subject><issn>0049-3848</issn><issn>1879-2472</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMtKAzEUhoMotVbfQKELEQVHT26TyUaQ4g0KbnQdMpmERuaiybTg25txSt1J4GTxf-fw8yF0iuEGA85vAZjMaMGKS4mvJNC8yMQemuJCyIwwQfbRdIccoqMYPwCwwJJP0ARLkgMXU3S9WHW1b-3ctytf-t537bxz88_Q9avQNaVv59r0fqOH5BgdOF1He7L9Z-j98eFt8ZwtX59eFvfLzNAi7zMiMCeMMkxE6XDhLAdOnNRpWg0VYEdkqR0IKHkBJXVGQp6aci4ptcLSGboY76YaX2sbe9X4aGxd69Z266gEwZzi9GaIjaAJXYzBOvUZfKPDt8KgBklqMKAGA0pi9StJibR2tr2_Lhtb_S2NVlJ-vs11NLp2QbfGxx3GZJ4zDgm7GzGbXGy8DSoab1tjKx-s6VXV-f97_AABlYDW</recordid><startdate>19910615</startdate><enddate>19910615</enddate><creator>Leach, Richard D.</creator><creator>Dewind, Sally A.</creator><creator>Slattery, Charles W.</creator><creator>Herrmann, E.Clifford</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>19910615</creationdate><title>Choline inhibition of prothrombin activation</title><author>Leach, Richard D. ; Dewind, Sally A. ; Slattery, Charles W. ; Herrmann, E.Clifford</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c386t-27152434127bf18fe5052f9a052ea0d01f29baf070b580b3fc90604955933e7e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>anticoagulant</topic><topic>Aspirin - pharmacology</topic><topic>Biological and medical sciences</topic><topic>Blood coagulation. Blood cells</topic><topic>Calcium - pharmacology</topic><topic>choline</topic><topic>Choline - pharmacology</topic><topic>chromogenic peptide substrate</topic><topic>Coagulation factors</topic><topic>Dipeptides - pharmacology</topic><topic>Enzyme Activation - drug effects</topic><topic>enzyme inhibitor</topic><topic>factor Va</topic><topic>Factor Xa Inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>Kinetics</topic><topic>Liposomes</topic><topic>Microcomputers</topic><topic>Molecular and cellular biology</topic><topic>Phospholipids - pharmacology</topic><topic>Prothrombin - metabolism</topic><topic>prothrombinase</topic><topic>Spectrophotometry</topic><topic>Thromboplastin - antagonists & inhibitors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Leach, Richard D.</creatorcontrib><creatorcontrib>Dewind, Sally A.</creatorcontrib><creatorcontrib>Slattery, Charles W.</creatorcontrib><creatorcontrib>Herrmann, E.Clifford</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>Leach, Richard D.</au><au>Dewind, Sally A.</au><au>Slattery, Charles W.</au><au>Herrmann, E.Clifford</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Choline inhibition of prothrombin activation</atitle><jtitle>Thrombosis research</jtitle><addtitle>Thromb Res</addtitle><date>1991-06-15</date><risdate>1991</risdate><volume>62</volume><issue>6</issue><spage>635</spage><epage>648</epage><pages>635-648</pages><issn>0049-3848</issn><eissn>1879-2472</eissn><coden>THBRAA</coden><abstract>A computer-interfaced spectrophotometric kinetic assay for prothrombin activation was developed, coupling the production of thrombin to a thrombin-specific amidolytic chromogenic reaction. As thrombin accumulated initially at constant velocity, the simultaneous release from S-2238 of pNA conformed to an acceleration function. Adherence to the acceleration function of the temporally increasing
A
400 of pNA was evaluated after transforming the data into linear format which permitted linear regression analysis. High correlation coefficients, routinely >0.99, verified linearity of thrombin production in individual assay mixtures. As prothrombin concentrations were varied, factor Xa exhibited Michaelis-Menten kinetics. Added choline produced a pattern of mixed-type inhibition. Replots of LB slopes and intercepts versus choline concentration gave apparent
K
i
and
K
i
values (mM): 22±3 and 48±7 without factor Va, 25±4 and 41±4 with factor Va.</abstract><cop>New York, NY</cop><pub>Elsevier Ltd</pub><pmid>1926057</pmid><doi>10.1016/0049-3848(91)90368-7</doi><tpages>14</tpages></addata></record> |
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| issn | 0049-3848 1879-2472 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | anticoagulant Aspirin - pharmacology Biological and medical sciences Blood coagulation. Blood cells Calcium - pharmacology choline Choline - pharmacology chromogenic peptide substrate Coagulation factors Dipeptides - pharmacology Enzyme Activation - drug effects enzyme inhibitor factor Va Factor Xa Inhibitors Fundamental and applied biological sciences. Psychology Humans Kinetics Liposomes Microcomputers Molecular and cellular biology Phospholipids - pharmacology Prothrombin - metabolism prothrombinase Spectrophotometry Thromboplastin - antagonists & inhibitors |
| title | Choline inhibition of prothrombin activation |
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