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Proteomic profile of the venom of three dark-colored Tityus (Scorpiones: Buthidae) from the tropical rainforests of Costa Rica
(2023)
Objective: We aimed to elucidate the potential differences in the venom peptide sequences of three Tityus species
from Costa Rican rainforests: T. jaimei, T. championi and T. dedoslargos, compared to T. cf. asthenes ...
Structure of myotoxin-II, a catalytically inactive Lys49 phospholipase A2 homologue from Atropoides nummifer venom
(2006)
Lys49 snake-venom phospholipase A2 (PLA2) homologues are highly myotoxic
proteins which, although lacking catalytic activity, possess the ability to disrupt
biological membranes, inducing significant muscle-tissue loss ...
Differential susceptibility of C2C12 myoblasts and myotubes to group II phospholipase A2 myotoxins from crotalid snake venoms
(2005)
Group II phospholipase A2 (PLA2) myotoxins isolated from Viperidae/Crotalidae snake venoms induce a rapid cytolytic
effect upon diverse cell types in vitro. Previous studies suggested that this effect could be more ...
Porcentaje y cifra absoluta de linfocitos T en sangre periférica por el método de rosetas E: estudio de cuarenta adultos sanos
(1985)
Se realizó la determinación del porcentaje y cifra absoluta de linfocitos T en sangre periférica a un grupo de 40 adultos sanos costarricenses, seleccionados de un grupo inicial de 58 voluntarios. Se utilizó un método de ...
Neutralization of myotoxic phospholipases A2 from the venom of the snake Bothrops asper by monoclonal antibodies
(1992)
The neutralization of two myotoxic phospholipases A2 from the venom of Bothrops asper, myotoxins I and II, by two murine monoclonal antibodies is reported. The monoclonal antibodies, MAb-3 and Mab-4, recognize different ...
The Phospholipase A2 Homologues of Snake Venoms: Biological Activities and Their Possible Adaptive Roles
(2009)
A particular subgroup of toxins with phospholipase A2 (PLA2) structure, but devoid of this enzymatic activity, is commonly found in the venoms of snakes of the family Viperidae, and known as the PLA2 homologues. Among ...
Cytotoxicity of snake venom Lys49 PLA2-like myotoxin on rat cardiomyocytes ex vivo does not involve a direct action on the contractile apparatus
(2021-09)
Viperid snake venoms contain a unique family of cytotoxic proteins, the Lys49 PLA2 homologs, which are devoid of enzymatic activity but disrupt the integrity of cell membranes. They are known to induce skeletal muscle ...
Cleavage of the NH2-Terminal Octapeptide of Bothrops asper Myotoxic Lysine-49 Phospholipase A2 Reduces Its Membrane-Destabilizing Effect
(1994-08)
Bothrops asper myotoxin II was cleaved with cyanogen bromide to determine the role of NH2-terminal amino acid residues in its ability to destabilize negatively charged liposomes and to induce myonecrosis. After treatment, ...
Tyr→Trp-substituted peptide 115-129 of a Lys49 phospholipase A2 expresses enhanced membrane-damaging activities and reproduces its in vivo myotoxic effect
(1999)
Myotoxin II is a group II Lys49 phospholipase A2 (PLA2) isolated from the venom of the snake Bothrops asper. Previous
studies on a synthetic peptide derived from its heparin-binding, cationic/hydrophobic sequence 115^129 ...
Identification of the myotoxic site of the Lys49 phospholipase A2 from Agkistrodon piscivorus piscivorus snake venom: synthetic C-terminal peptides from Lys49, but not from Asp49 myotoxins, exert membrane-damaging activities
(2001)
Group II phospholipase A2 (PLA2) myotoxins found in the venoms of Crotalidae snakes can be divided into `Asp49' and
`Lys49' isoforms, the latter being considered catalytically-inactive variants. Previous studies on one ...