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Biochemical Characterization, Action on Macrophages, and Superoxide Anion Production of Four Basic Phospholipases A 2 from Panamanian Bothrops asper Snake Venom
Bothrops asper (Squamata: Viperidae) is the most important venomous snake in Central America, being responsible for the majority of snakebite accidents. Four basic PLA 2 s (pMTX-I to -IV) were purified from crude venom by a single-step chromatography using a CM-Sepharose ion-exchange column (1.5 × 1...
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Published in: | BioMed research international 2013, Vol.2013, p.1-9 |
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Main Authors: | , , , , , , , |
Format: | Article |
Language: | English |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Bothrops asper
(Squamata: Viperidae) is the most important venomous snake in Central America, being responsible for the majority of snakebite accidents. Four basic PLA
2
s (pMTX-I to -IV) were purified from crude venom by a single-step chromatography using a CM-Sepharose ion-exchange column (1.5 × 15 cm). Analysis of the N-terminal sequence demonstrated that pMTX-I and III belong to the catalytically active Asp49 phospholipase A
2
subclass, whereas pMTX-II and IV belong to the enzymatically inactive Lys49 PLA
2
s-like subclass. The PLA
2
s isolated from Panama
Bothrops asper
venom (pMTX-I, II, III, and IV) are able to induce myotoxic activity, inflammatory reaction mainly leukocyte migration to the muscle, and induce J774A.1 macrophages activation to start phagocytic activity and superoxide production. |
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ISSN: | 2314-6133 2314-6141 |
DOI: | 10.1155/2013/789689 |