In vitro antiplasmodial activity of phospholipases A2 and a phospholipase homologue isolated from the venom of the snake Bothrops asper

The antimicrobial and antiparasite activity of phospholipase A2 (PLA2) from snakes and bees has been extensively explored. We studied the antiplasmodial effect of the whole venom of the snake Bothrops asper and of two fractions purified by ion-exchange chromatography: one containing catalytically-ac...

Full description

Autores:

Quintana Castillo, Juan Carlos
Vargas L.J.
Segura C.
Gutiérrez J.M.
Pérez J.C.A.

Tipo de recurso:

Article of journal

Fecha de publicación:

2012

Institución:

Universidad Cooperativa de Colombia

Repositorio:

Repositorio UCC

Idioma:

OAI Identifier:

oai:repository.ucc.edu.co:20.500.12494/42902

Acceso en línea:

https://doi.org/10.7149/OPA.51.3.50306
https://www.sciencedirect.com/science/article/abs/pii/S0034745014601463
https://hdl.handle.net/20.500.12494/42902

Palabra clave:

phospholipase
phospholipase A2
snake venom
acute toxicity
amino acid sequence
antimalarial activity
antiplasmodial activity
article
bothrops asper
cell fractionation
controlled study
cytotoxicity
drug activity
enzyme active site
enzyme activity
hemolysis
IC 50
in vitro study
ion exchange chromatography
LD 50
lethality
nonhuman
nucleotide sequence
peripheral blood mononuclear cell
Plasmodium falciparum
sequence alignment
snake
toxicity testing
Amino Acid Sequence
Animals
Antiprotozoal Agents
Bothrops
Cell Survival
Cells
Cultured
Crotalid Venoms
Erythrocytes
Humans
Lethal Dose 50
Leukocytes
Mononuclear
Mice
Molecular Sequence Data
Phospholipases
Plasmodium falciparum
Sequence Alignment

Rights

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License

http://purl.org/coar/access_right/c_14cb