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

Rosalina Inga; Dan Vivas; Pedro Palermo; Julio Mendoza; Fanny Lazo; Armando Yarlequé

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

Translated title of the contribution: Caracterización biológica y acción de inhibidores de una fosfolipasa A₂ del veneno de Lachesis muta

Rosalina Inga, Dan Vivas, Pedro Palermo, Julio Mendoza, Fanny Lazo, Armando Yarlequé

Research output: Contribution to journal › Article › peer-review

Abstract

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.

Translated title of the contribution	Caracterización biológica y acción de inhibidores de una fosfolipasa A₂ del veneno de Lachesis muta
Original language	Spanish
Pages (from-to)	123-128
Number of pages	6
Journal	Revista Peruana de Biologia
Volume	17
Issue number	1
State	Published - Apr 2010

Bibliographical note

Funding Information:
Trabajo presentado a la XVIII Reunión Científica del Instituto de Investigaciones en Ciencias Bioló- gicas Antonio Raimondi, “200 años del nacimiento de Charles Darwin y el 150 aniversario de la publicación de On the Origin of Species by Means of Natural Selection”. Del 19 al 21 de agosto de 2009.

Publisher Copyright:
© Facultad de Ciencias Biológicas UNMSM

Cite this

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abstract = "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.",

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AU - Inga, Rosalina

AU - Vivas, Dan

AU - Palermo, Pedro

AU - Mendoza, Julio

AU - Lazo, Fanny

AU - Yarlequé, Armando

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AB - 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.

KW - Enzyme

KW - Inhibition

KW - Phospholipase A2

KW - Snake

KW - Toxicity

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

Abstract

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