Structural and functional characterization of myotoxin I, a Lys49 phospholipase A2 homologue from Bothrops moojeni (Caissaca) snake venom

AM Soares, SH Andrião-Escarso, Y Angulo… - Archives of Biochemistry …, 2000 - Elsevier
Myotoxin-I (MjTX-I) was purified to homogeneity from the venom of Bothrops moojeni by ion-
exchange chromatography on CM-Sepharose. Its molecular weight, estimated by SDS …

Analysis of Bothrops jararacussu venomous gland transcriptome focusing on structural and functional aspects: I—gene expression profile of highly expressed …

S Kashima, PG Roberto, AM Soares, S Astolfi-Filho… - Biochimie, 2004 - Elsevier
Snake venom glands are a rich source of bioactive molecules such as peptides, proteins
and enzymes that show important pharmacological activity leading to in local and systemic …

Inhibition of the Myotoxicity Induced by Bothrops jararacussu Venom and Isolated Phospholipases A2 by Specific Camelid Single-Domain Antibody Fragments

NDR Prado, SS Pereira, MP da Silva, MSS Morais… - PLoS …, 2016 - journals.plos.org
Antivenoms, produced using animal hyperimmune plasma, remains the standard therapy for
snakebites. Although effective against systemic damages, conventional antivenoms have …

Renal toxicity of Bothrops moojeni snake venom and its main myotoxins

PSF Barbosa, A Havt, PEG Facó, TM Sousa, I Bezerra… - Toxicon, 2002 - Elsevier
Acute renal failure is one the most common systemic complications after snakebite,
however, its pathogenesis remains obscure. In this study we evaluated the renal effects of …

Inhibition of the myotoxic activity of Bothrops jararacussu venom and its two major myotoxins, BthTX-I and BthTX-II, by the aqueous extract of Tabernaemontana …

ELG Veronese, LE Esmeraldino, APF Trombone… - Phytomedicine, 2005 - Elsevier
Partial neutralization of the myotoxic effect of Bothrops jararacussu venom (BV) and two of
its myotoxins [bothropstoxin-I (BthTX-I), catalytically inactive, and II (BthTX-II), showing low …

Isolation, characterization and biological activity of acidic phospholipase A2 isoforms from Bothrops jararacussu snake venom

DFJ Ketelhut, MH De Mello, ELG Veronese… - Biochimie, 2003 - Elsevier
Acidic phospholipase A2 (PLA2) isoforms in snake venoms, particularly those from Bothrops
jararacussu, have not been characterized. This article reports the isolation and partial …

Phenotypic, functional and plasticity features of human PBMCs induced by venom secreted PLA2s

JA Lopes, CN Boeno, MV Paloschi, MDS Silva… - Molecular …, 2023 - Elsevier
Bothrops venom contains a high amount of secreted phospholipase A 2 (sPLA 2 s) enzymes
responsible for the inflammatory reaction and activation of leukocytes in cases of …

Biological and biochemical characterization of new basic phospholipase A2 BmTX-I isolated from Bothrops moojeni snake venom

AK Calgarotto, DCS Damico, LA Ponce-Soto… - Toxicon, 2008 - Elsevier
BmTX-I, an Asp49 phospholipase A2, was purified from Bothrops moojeni venom after only
one chromatographic step using reverse-phase HPLC on μ-Bondapak C-18 column. A …

[HTML][HTML] Isolation and functional characterization of proinflammatory acidic phospholipase A2 from Bothrops leucurus snake venom

DCO Nunes, RS Rodrigues, MN Lucena… - … and Physiology Part C …, 2011 - Elsevier
In the present study, an acidic PLA2, designated Bl-PLA2, was isolated from Bothrops
leucurus snake venom through two chromatographic steps: ion-exchange on CM …

Structural, functional, and bioinformatics studies reveal a new snake venom homologue phospholipase A2 class

JI dos Santos, M Cintra‐Francischinelli… - Proteins: Structure …, 2011 - Wiley Online Library
Abstract Phospholipases A2 (PLA2s) are enzymes responsible for membrane disruption
through Ca2+‐dependent hydrolysis of phospholipids. Lys49‐PLA2s are well‐characterized …