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

Authors

  • Rosalina Inga Laboratorio de Biología Molecular, Facultad de Ciencias Biológicas, Universidad Nacional Mayor de San Marcos. Apartado 11-0058, Lima 11, Perú.
  • Dan Vivas Laboratorio de Biología Molecular, Facultad de Ciencias Biológicas, Universidad Nacional Mayor de San Marcos. Apartado 11-0058, Lima 11, Perú.
  • Pedro Palermo Laboratorio de Biología Molecular, Facultad de Ciencias Biológicas, Universidad Nacional Mayor de San Marcos. Apartado 11-0058, Lima 11, Perú.
  • Julio Mendoza Laboratorio de Biología Molecular, Facultad de Ciencias Biológicas, Universidad Nacional Mayor de San Marcos. Apartado 11-0058, Lima 11, Perú.
  • Fanny Lazo Laboratorio de Biología Molecular, Facultad de Ciencias Biológicas, Universidad Nacional Mayor de San Marcos. Apartado 11-0058, Lima 11, Perú.
  • Armando Yarlequé Laboratorio de Biología Molecular, Facultad de Ciencias Biológicas, Universidad Nacional Mayor de San Marcos. Apartado 11-0058, Lima 11, Perú.

DOI:

https://doi.org/10.15381/rpb.v17i1.60

Keywords:

Phospholipase A2, enzyme, snake, toxicity, inhibition.

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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Published

04/19/2010

Issue

Vol. 17 No. 1 (2010)

Section

Articles

License

Copyright (c) 2010 Rosalina Inga, Dan Vivas, Pedro Palermo, Julio Mendoza, Fanny Lazo, Armando Yarlequé

Creative Commons License

This work is licensed under a Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International License.

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How to Cite

Inga, Rosalina, Dan Vivas, Pedro Palermo, Julio Mendoza, Fanny Lazo, and Armando Yarlequé. 2010. “Biological Characterization and Inhibitors Action of Phospholipase A2 from Lachesis Muta Venom”. Revista Peruana De Biología 17 (1): 123-28. https://doi.org/10.15381/rpb.v17i1.60.