Activación y determinación de parámetros cinéticos de la Plasmina Humana y Ovis aries

Autores:: Cañas, Omaira
Quijano, Alfonso
Arbeláez, Fernando

Tipo de recurso:: Article of journal

Fecha de publicación:: 2010

Institución:: Universidad de Córdoba

Repositorio:: Repositorio Institucional Unicórdoba

Idioma:: spa

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dc.title.spa.fl_str_mv	Activación y determinación de parámetros cinéticos de la Plasmina Humana y Ovis aries
dc.title.translated.eng.fl_str_mv	Activación y determinación de parámetros cinéticos de la Plasmina Humana y Ovis aries
title	Activación y determinación de parámetros cinéticos de la Plasmina Humana y Ovis aries
spellingShingle	Activación y determinación de parámetros cinéticos de la Plasmina Humana y Ovis aries Plasmin Glu–Plasminogen fibrinolysis urokinase kinetics.
title_short	Activación y determinación de parámetros cinéticos de la Plasmina Humana y Ovis aries
title_full	Activación y determinación de parámetros cinéticos de la Plasmina Humana y Ovis aries
title_fullStr	Activación y determinación de parámetros cinéticos de la Plasmina Humana y Ovis aries
title_full_unstemmed	Activación y determinación de parámetros cinéticos de la Plasmina Humana y Ovis aries
title_sort	Activación y determinación de parámetros cinéticos de la Plasmina Humana y Ovis aries
dc.creator.fl_str_mv	Cañas, Omaira Quijano, Alfonso Arbeláez, Fernando
dc.contributor.author.spa.fl_str_mv	Cañas, Omaira Quijano, Alfonso Arbeláez, Fernando
dc.subject.spa.fl_str_mv	Plasmin Glu–Plasminogen fibrinolysis urokinase kinetics.
topic	Plasmin Glu–Plasminogen fibrinolysis urokinase kinetics.
publishDate	2010
dc.date.issued.none.fl_str_mv	2010-01-01
dc.date.accessioned.none.fl_str_mv	2011-01-01 00:00:00 2022-07-01T20:58:54Z
dc.date.available.none.fl_str_mv	2011-01-01 00:00:00 2022-07-01T20:58:54Z
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dc.identifier.doi.none.fl_str_mv	10.21897/rmvz.295
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dc.identifier.eissn.none.fl_str_mv	1909-0544
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dc.relation.references.spa.fl_str_mv	Kleinschnitz C, Stoll M, Bendszus K, Schuh H, Pauer P, Burfeind C et al. Targeting coagulation factor XII provides protection from pathological thrombosis in cerebral ischemia without interfering with hemostasis. J Exp Med 2006; 203:513–518. http://dx.doi.org/10.1084/jem.20052458 Mackman N. Role of tissue factor in hemostasis thrombosis, and vascular development. Arterioscler Thromb Vasc Biol 2004; 24:1015–1022. http://dx.doi.org/10.1161/01.ATV.0000130465.23430.74 Whelihan MF, Orfeo T, Gissel MT, Mann KG. Coagulation procofactor activation by factor XIa. J Thromb Haemost 2010; 7:1532–1539. http://dx.doi.org/10.1111/j.1538-7836.2010.03899.x Kolodziejczyk J, Wachowicz B. Dysfunction of fibrinolysis as a risk factor of thrombosis. Pol Merkur Lekarski 2009; 160:341–5. Zhang L, Seiffert D, Fowler BJ, Jenkins GR, Thinnes TC, Loskutoff DJ, Parmer RJ, Miles LA. Plasminogen has a broad extrahepatic distributions. Thromb Haemost 2002; 87:493–501. Kouemo S, McMillan E, Doctor V. Mechanism of the synergistic effect between oversulfated chondroitin–6–sulfate and lysine or 6–aminohexanoic acid in enhancing the in–vitro activation of glutamic plasminogen by tissue plasminogen activator or urokinase. Blood Coagul Fibrinolysis 2010; 21:425–430. http://dx.doi.org/10.1097/MBC.0b013e328337b436 Walter NG. Michaelis–Menten is dead, long live Michaelis–Menten!. Nat chem Biol 2006; 2:66–67. http://dx.doi.org/10.1038/nchembio0206-66 Ca-as O, Quijano A, Arbeláez LF. Activación y cinética comparativa de dos especies de Plasminógenos: Humano y Bovino. Bistua 2006; 4:3–12. Ca-as O, Quijano A, Arbeláez LF. Cinética comparativa de la Plasmina canina con la humana, bovina y equina. Bistua 2007; 5:17–24. Ca-as O, Quijano A, Arbeláez LF. Activación y Cinética comparativa de la Plasmina Bufalina con la humana. Rev Col Cien Pec 2010; 23:47–54. Longstaff C, Whitton CM. Aproposed reference method for plasminogen activators that enables calculation of enzyme activities in SI units. J Thromb Haemost 2004; 2:1416–1421. http://dx.doi.org/10.1111/j.1538-7836.2004.00816.x Chakavarti B, Chakavarti D. Electrophoretic separation of proteins. J vis Exp 2008; 16:3791–758. http://dx.doi.org/10.3791/758 Oe T, Maekawa M, Satoh R, Lee SH, Goto T. Combining [13C6]–phenylisothiocyanate and the Edman degradation reaction: a possible breakthrough for absolute quantitative proteomics together with protein identification. Rapid commun mass spectrom 2010; 2:173–9. http://dx.doi.org/10.1002/rcm.4372 Christensen B, Schack L, Kläning E, Sørensen ES. Osteopontin is cleaved at multiple sites close to its integrin–binding motifs in milk and is a novel substrate for plasmin and cathepsin D. J Biol Chem 2010; 285:7929–37. http://dx.doi.org/10.1074/jbc.M109.075010 Weinberg ML, Felicori LF, Bello CA, Magalhaes HP, Almeida AP, Magalhaes A, Sanchez EF. Biochemical properties of a bushmaster snake venom serine proteinase (LV–Ka) and its kinin releasing activity evaluated in rat mesenteric arterial rings. J Pharmacol Sci 2004; 96:333–42 http://dx.doi.org/10.1254/jphs.FPJ04005X Daviglus ML, Lloyd–jones DM, Pirzada A. Preventing cardiovascular disease in the 21st century: therapeutic and preventive implications of current evidence. Am J Cardiovasc Drugs 2006; 6:87–101. http://dx.doi.org/10.2165/00129784-200606020-00003 Weisel JW. Fibrinogen and fibrin. Adv Protein Chem 2005; 70:247–99. http://dx.doi.org/10.1016/S0065-3233(05)70008-5
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dc.relation.citationedition.spa.fl_str_mv	Núm. 1 , Año 2011 : Revista MVZ Córdoba Volumen 16(1) Enero-Abril 2011
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dc.relation.ispartofjournal.spa.fl_str_mv	Revista MVZ Córdoba
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dc.publisher.spa.fl_str_mv	Universidad de Córdoba
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spelling	Cañas, Omairab942c93a-5b0f-41c2-a308-95643a297ad8-1Quijano, Alfonso11a83aaf-5323-4ddc-9493-a63de055195a-1Arbeláez, Fernandoc9551311-9278-4629-aa01-caea791249f6-12011-01-01 00:00:002022-07-01T20:58:54Z2011-01-01 00:00:002022-07-01T20:58:54Z2010-01-010122-0268https://repositorio.unicordoba.edu.co/handle/ucordoba/551610.21897/rmvz.295https://doi.org/10.21897/rmvz.2951909-0544application/pdfspaUniversidad de Córdobahttps://creativecommons.org/licenses/by-nc-sa/4.0/info:eu-repo/semantics/openAccesshttp://purl.org/coar/access_right/c_abf2https://revistamvz.unicordoba.edu.co/article/view/295PlasminGlu–Plasminogenfibrinolysisurokinasekinetics.Activación y determinación de parámetros cinéticos de la Plasmina Humana y Ovis ariesActivación y determinación de parámetros cinéticos de la Plasmina Humana y Ovis ariesArtículo de revistaJournal articleinfo:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501http://purl.org/coar/resource_type/c_6501http://purl.org/coar/resource_type/c_2df8fbb1info:eu-repo/semantics/publishedVersionTexthttp://purl.org/redcol/resource_type/ARTREFhttp://purl.org/coar/version/c_970fb48d4fbd8a85Kleinschnitz C, Stoll M, Bendszus K, Schuh H, Pauer P, Burfeind C et al. Targeting coagulation factor XII provides protection from pathological thrombosis in cerebral ischemia without interfering with hemostasis. J Exp Med 2006; 203:513–518. http://dx.doi.org/10.1084/jem.20052458Mackman N. Role of tissue factor in hemostasis thrombosis, and vascular development. Arterioscler Thromb Vasc Biol 2004; 24:1015–1022. http://dx.doi.org/10.1161/01.ATV.0000130465.23430.74Whelihan MF, Orfeo T, Gissel MT, Mann KG. Coagulation procofactor activation by factor XIa. J Thromb Haemost 2010; 7:1532–1539. http://dx.doi.org/10.1111/j.1538-7836.2010.03899.xKolodziejczyk J, Wachowicz B. Dysfunction of fibrinolysis as a risk factor of thrombosis. Pol Merkur Lekarski 2009; 160:341–5.Zhang L, Seiffert D, Fowler BJ, Jenkins GR, Thinnes TC, Loskutoff DJ, Parmer RJ, Miles LA. Plasminogen has a broad extrahepatic distributions. Thromb Haemost 2002; 87:493–501.Kouemo S, McMillan E, Doctor V. Mechanism of the synergistic effect between oversulfated chondroitin–6–sulfate and lysine or 6–aminohexanoic acid in enhancing the in–vitro activation of glutamic plasminogen by tissue plasminogen activator or urokinase. Blood Coagul Fibrinolysis 2010; 21:425–430. http://dx.doi.org/10.1097/MBC.0b013e328337b436Walter NG. Michaelis–Menten is dead, long live Michaelis–Menten!. Nat chem Biol 2006; 2:66–67. http://dx.doi.org/10.1038/nchembio0206-66Ca-as O, Quijano A, Arbeláez LF. Activación y cinética comparativa de dos especies de Plasminógenos: Humano y Bovino. Bistua 2006; 4:3–12.Ca-as O, Quijano A, Arbeláez LF. Cinética comparativa de la Plasmina canina con la humana, bovina y equina. Bistua 2007; 5:17–24.Ca-as O, Quijano A, Arbeláez LF. Activación y Cinética comparativa de la Plasmina Bufalina con la humana. Rev Col Cien Pec 2010; 23:47–54.Longstaff C, Whitton CM. Aproposed reference method for plasminogen activators that enables calculation of enzyme activities in SI units. J Thromb Haemost 2004; 2:1416–1421. http://dx.doi.org/10.1111/j.1538-7836.2004.00816.xChakavarti B, Chakavarti D. Electrophoretic separation of proteins. J vis Exp 2008; 16:3791–758. http://dx.doi.org/10.3791/758Oe T, Maekawa M, Satoh R, Lee SH, Goto T. Combining [13C6]–phenylisothiocyanate and the Edman degradation reaction: a possible breakthrough for absolute quantitative proteomics together with protein identification. Rapid commun mass spectrom 2010; 2:173–9. http://dx.doi.org/10.1002/rcm.4372Christensen B, Schack L, Kläning E, Sørensen ES. Osteopontin is cleaved at multiple sites close to its integrin–binding motifs in milk and is a novel substrate for plasmin and cathepsin D. J Biol Chem 2010; 285:7929–37. http://dx.doi.org/10.1074/jbc.M109.075010Weinberg ML, Felicori LF, Bello CA, Magalhaes HP, Almeida AP, Magalhaes A, Sanchez EF. Biochemical properties of a bushmaster snake venom serine proteinase (LV–Ka) and its kinin releasing activity evaluated in rat mesenteric arterial rings. J Pharmacol Sci 2004; 96:333–42 http://dx.doi.org/10.1254/jphs.FPJ04005XDaviglus ML, Lloyd–jones DM, Pirzada A. Preventing cardiovascular disease in the 21st century: therapeutic and preventive implications of current evidence. Am J Cardiovasc Drugs 2006; 6:87–101. http://dx.doi.org/10.2165/00129784-200606020-00003Weisel JW. Fibrinogen and fibrin. Adv Protein Chem 2005; 70:247–99. http://dx.doi.org/10.1016/S0065-3233(05)70008-5https://revistamvz.unicordoba.edu.co/article/download/295/363Núm. 1 , Año 2011 : Revista MVZ Córdoba Volumen 16(1) Enero-Abril 2011116Revista MVZ CórdobaPublicationOREORE.xmltext/xml2596https://repositorio.unicordoba.edu.co/bitstreams/b8ca1bf6-7b0d-4af9-977f-444a90e62ec6/download82cd63a152d7f02681b458451c52b5ddMD51ucordoba/5516oai:repositorio.unicordoba.edu.co:ucordoba/55162023-10-06 00:46:36.217https://creativecommons.org/licenses/by-nc-sa/4.0/metadata.onlyhttps://repositorio.unicordoba.edu.coRepositorio Universidad de Córdobabdigital@metabiblioteca.com

Activación y determinación de parámetros cinéticos de la Plasmina Humana y Ovis aries

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