Now showing items 61-66 of 66
Characterization of a basic phospholipase A2-homologue myotoxin isolated from the venom of the snake Bothrops neuwiedii (yarará chica) from Argentina
A basic protein was isolated by CM-Sephadex C-25 chromatography from the venom of Bothrops neuwiedii from Argentina, and named B. neuwiedii myotoxin I. This protein exerted local myotoxic and edema-forming e ects in mice, ...
Structural characterization and phylogenetic relationships of myotoxin II from Atropoides (Bothrops) nummifer snake venom, a Lys49 phospholipase A2 homologue
In order to analyze its structure–function relationships, the complete amino acid sequence of myotoxin II from Atropoides (Bothrops) nummifer from Costa Rica was determined. This toxin is a Lys49-type phospholipase A2 ...
An overview of Lysine-49 phospholipase A2 myotoxins from crotalid snake venoms and their structural determinants of myotoxic action
In 1984, the first venom phospholipase A2 (PLA2) with a lysine substituting for the highly conserved aspartate 49 was discovered, in the North American crotalid snake Agkistrodon p. piscivorus [J. Biol. Chem. 259 (1984) ...
Immunochemical properties of the N-terminal helix of myotoxin II, a lysine-49 phospholipase A2 from Bothrops asper snake venom
Myotoxic class II phospholipases A2 from snake venoms can be divided into Asp49 and Lys49 types. The latter, including Bothrops asper myotoxin II, exert membrane damage despite lacking catalytic activity. A heparin-binding, ...
Neutralization of Bothrops asper venom by antibodies, natural products, and synthetic drugs: contributions to understanding snakebite envenomings and their treatment
Interest in studies on the neutralization of snake venoms and toxins by diverse types of inhibitors is two-fold. From an applied perspective, results enclose the potential to be translated into useful therapeutic products ...
Antimicrobial activity of myotoxic phospholipases A2 from crotalid snake venoms and synthetic peptide variants derived from their C-terminal region
A short peptide derived from the C-terminal region of Bothrops asper myotoxin II, a Lys49 phospholipase A2 (PLA2), was previously found to reproduce the bactericidal activity of its parent molecule. In this study, a panel ...