Biological characterization and inhibitors action of Phospholipase A2 from Lachesis muta venom

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In the present study, phospholipase A2 (PLA2) from Lachesis muta (Linnaeus, 1766), is isolated, purified and characterized biochemically and biologically. Purification was performed by liquid chromatography (LC) using CM-Sephadex C-50 and Sephadex G-50, homogenized enzyme had a molecular weight of 1...

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Detalles Bibliográficos
Autores: Inga, Rosalina, Vivas, Dan, Palermo, Pedro, Mendoza, Julio, Lazo, Fanny, Yarlequé, Armando
Formato: artículo
Fecha de Publicación:2010
Institución:Universidad Nacional Mayor de San Marcos
Repositorio:Revistas - Universidad Nacional Mayor de San Marcos
Lenguaje:español
OAI Identifier:oai:ojs.csi.unmsm:article/60
Enlace del recurso:https://revistasinvestigacion.unmsm.edu.pe/index.php/rpb/article/view/60
Nivel de acceso:acceso abierto
Materia:Fosfolipasa A2
enzima
ofidio
toxicidad
inhibición.
Phospholipase A2
enzyme
snake
toxicity
inhibition.
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spelling Biological characterization and inhibitors action of Phospholipase A2 from Lachesis muta venomCaracterización biológica y acción de inhibidores de una fosfolipasa A2 del veneno de Lachesis mutaInga, RosalinaVivas, DanPalermo, PedroMendoza, JulioLazo, FannyYarlequé, ArmandoFosfolipasa A2enzimaofidiotoxicidadinhibición.Phospholipase A2enzymesnaketoxicityinhibition.In the present study, phospholipase A2 (PLA2) from Lachesis muta (Linnaeus, 1766), is isolated, purified and characterized biochemically and biologically. Purification was performed by liquid chromatography (LC) using CM-Sephadex C-50 and Sephadex G-50, homogenized enzyme had a molecular weight of 18749 Da. Trials with egg yolk phospholipids, and commercial lecithin showed that EDTA, PMSF, glutathione and cysteine inhibited the activity with values greater than 50%. The PLA2 had a significant anticoagulant effect, showing a delay of 2'30" on the coagulation time with 9.6 µg of the enzyme. The indirect impact on human erythrocyte hemolysis gave an equivalent of 4.35 µg as HD50. Mean edematic dose and minimum myotoxic dose were 91.5 mg and 125.89 mg / mL respectively, these values were below enzymes phospholipase A2 from others poisons. There was no hemorrhagic activity. Immunodiffusion tests and immunoelectrophoresis revealed that the PLA2 of L. muta was immunogenic reactivity against lachesic monovalent antivenom (INS-Peru). However, the neutralization by the antivenom was partial. El presente trabajo informa de la purificación y caracterización bioquímica y biológica de la fosfolipasa A2 (PLA2) de Lachesis muta (Linnaeus, 1766). La purificación se realizó por cromatografía liquida (CL) usando CM-Sephadex C-50 y Sephadex G-50, obteniéndola al estado homogéneo con un peso molecular de 18749 Da. Los ensayos con PLA2 realizados sobre fosfolípidos de yema de huevo y lecitina comercial, mostraron que los agentes EDTA, PMSF, glutatión y cisteína, inhibieron la actividad con valores mayores al 50%. La PLA2 de L. muta produjo un notable efecto anticoagulante, observándose un retardo de 2'30" en el tiempo de coagulación con 9,6 µg de la enzima. La hemólisis indirecta sobre eritrocitos humanos dio un equivalente de 4,35 µg como dosis hemolítica media (HD50). Los valores de dosis edemática media y dosis miotóxica mínima fueron de 91,5 µg y 125,89 µg/mL respectivamente; valores por debajo de PLA2 de otros venenos. No se registró actividad hemorrágica directa. Las pruebas de inmunodifusión e inmunoelectroforésis revelaron que PLA2 de L. muta tuvo reactividad inmunogénica contra el antiveneno lachésico monovalente (INS-Perú). Sin embargo, la neutralización por el antiveneno fue parcial.Universidad Nacional Mayor de San Marcos, Facultad de Ciencias Biológicas2010-04-19info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://revistasinvestigacion.unmsm.edu.pe/index.php/rpb/article/view/6010.15381/rpb.v17i1.60Revista Peruana de Biología; Vol. 17 Núm. 1 (2010); 123 - 128Revista Peruana de Biología; Vol. 17 No. 1 (2010); 123 - 1281727-99331561-0837reponame:Revistas - Universidad Nacional Mayor de San Marcosinstname:Universidad Nacional Mayor de San Marcosinstacron:UNMSMspahttps://revistasinvestigacion.unmsm.edu.pe/index.php/rpb/article/view/60/55Derechos de autor 2010 Rosalina Inga, Dan Vivas, Pedro Palermo, Julio Mendoza, Fanny Lazo, Armando Yarlequéhttps://creativecommons.org/licenses/by-nc-sa/4.0info:eu-repo/semantics/openAccessoai:ojs.csi.unmsm:article/602020-05-21T18:07:59Z
dc.title.none.fl_str_mv Biological characterization and inhibitors action of Phospholipase A2 from Lachesis muta venom
Caracterización biológica y acción de inhibidores de una fosfolipasa A2 del veneno de Lachesis muta
title Biological characterization and inhibitors action of Phospholipase A2 from Lachesis muta venom
spellingShingle Biological characterization and inhibitors action of Phospholipase A2 from Lachesis muta venom
Inga, Rosalina
Fosfolipasa A2
enzima
ofidio
toxicidad
inhibición.
Phospholipase A2
enzyme
snake
toxicity
inhibition.
title_short Biological characterization and inhibitors action of Phospholipase A2 from Lachesis muta venom
title_full Biological characterization and inhibitors action of Phospholipase A2 from Lachesis muta venom
title_fullStr Biological characterization and inhibitors action of Phospholipase A2 from Lachesis muta venom
title_full_unstemmed Biological characterization and inhibitors action of Phospholipase A2 from Lachesis muta venom
title_sort Biological characterization and inhibitors action of Phospholipase A2 from Lachesis muta venom
dc.creator.none.fl_str_mv Inga, Rosalina
Vivas, Dan
Palermo, Pedro
Mendoza, Julio
Lazo, Fanny
Yarlequé, Armando
author Inga, Rosalina
author_facet Inga, Rosalina
Vivas, Dan
Palermo, Pedro
Mendoza, Julio
Lazo, Fanny
Yarlequé, Armando
author_role author
author2 Vivas, Dan
Palermo, Pedro
Mendoza, Julio
Lazo, Fanny
Yarlequé, Armando
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Fosfolipasa A2
enzima
ofidio
toxicidad
inhibición.
Phospholipase A2
enzyme
snake
toxicity
inhibition.
topic Fosfolipasa A2
enzima
ofidio
toxicidad
inhibición.
Phospholipase A2
enzyme
snake
toxicity
inhibition.
description In the present study, phospholipase A2 (PLA2) from Lachesis muta (Linnaeus, 1766), is isolated, purified and characterized biochemically and biologically. Purification was performed by liquid chromatography (LC) using CM-Sephadex C-50 and Sephadex G-50, homogenized enzyme had a molecular weight of 18749 Da. Trials with egg yolk phospholipids, and commercial lecithin showed that EDTA, PMSF, glutathione and cysteine inhibited the activity with values greater than 50%. The PLA2 had a significant anticoagulant effect, showing a delay of 2'30" on the coagulation time with 9.6 µg of the enzyme. The indirect impact on human erythrocyte hemolysis gave an equivalent of 4.35 µg as HD50. Mean edematic dose and minimum myotoxic dose were 91.5 mg and 125.89 mg / mL respectively, these values were below enzymes phospholipase A2 from others poisons. There was no hemorrhagic activity. Immunodiffusion tests and immunoelectrophoresis revealed that the PLA2 of L. muta was immunogenic reactivity against lachesic monovalent antivenom (INS-Peru). However, the neutralization by the antivenom was partial.
publishDate 2010
dc.date.none.fl_str_mv 2010-04-19
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://revistasinvestigacion.unmsm.edu.pe/index.php/rpb/article/view/60
10.15381/rpb.v17i1.60
url https://revistasinvestigacion.unmsm.edu.pe/index.php/rpb/article/view/60
identifier_str_mv 10.15381/rpb.v17i1.60
dc.language.none.fl_str_mv spa
language spa
dc.relation.none.fl_str_mv https://revistasinvestigacion.unmsm.edu.pe/index.php/rpb/article/view/60/55
dc.rights.none.fl_str_mv https://creativecommons.org/licenses/by-nc-sa/4.0
info:eu-repo/semantics/openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/4.0
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Universidad Nacional Mayor de San Marcos, Facultad de Ciencias Biológicas
publisher.none.fl_str_mv Universidad Nacional Mayor de San Marcos, Facultad de Ciencias Biológicas
dc.source.none.fl_str_mv Revista Peruana de Biología; Vol. 17 Núm. 1 (2010); 123 - 128
Revista Peruana de Biología; Vol. 17 No. 1 (2010); 123 - 128
1727-9933
1561-0837
reponame:Revistas - Universidad Nacional Mayor de San Marcos
instname:Universidad Nacional Mayor de San Marcos
instacron:UNMSM
instname_str Universidad Nacional Mayor de San Marcos
instacron_str UNMSM
institution UNMSM
reponame_str Revistas - Universidad Nacional Mayor de San Marcos
collection Revistas - Universidad Nacional Mayor de San Marcos
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 13.924177
Biological characterization and inhibitors action of Phospholipase A2 from Lachesis muta venom
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