Journal Article

Purification procedure for the isolation of a P-I metalloprotease and an acidic phospholipase A sub(2) fromBothrops atrox snake venom

Bernardes, Carolina P, Menaldo, Danilo L, Cintra, Adelia C O, Jacob-Ferreira, Anna L, Sampaio, Suely V

2015

Overview

Snake venoms are complex mixtures of inorganic and organic components, mainly proteins and peptides. Standardization of methods for isolating bioactive molecules from snake venoms is extremely difficult due to the complex and highly variable composition of venoms, which can be influenced by factors such as age and geographic location of the specimen. Therefore, this study aimed to standardize a simple purification methodology for obtaining a P-I class metalloprotease (MP) and an acidic phospholipase A2 (PLA 2 ) from Bothrops atroxvenom, and biochemically characterize these molecules to enable future functional studies. To obtain the toxins of interest, a method has been standardized using consecutive isolation steps. The present study successfully standardized a simple methodology to isolate the metalloprotease Batroxase and the acidic PLA 2 BatroxPLA2 from the venom of B. atrox, consisting mainly of classical chromatographic processes. These two enzymes will be used in future studies to evaluate their effects on the complement system and the inflammatory process, in addition to the thrombolytic potential of the metalloprotease.

• Subject: Bothrops