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Identification of linear B-cell epitopes on myotoxin-II, a Lys49 phospholipase A2 homologue from Bothrops asper snake venom
(2012)
Knowledge on toxin immunogenicity at the molecular level can provide valuable information
for the improvement of antivenoms, as well as for understanding toxin structure–
function relationships. The aims of this study ...
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 ...
High-density peptide microarray exploration of the antibody response in a rabbit immunized with a neurotoxic venom fraction
(2017-11)
Polyvalent snakebite antivenoms derive their therapeutic success from the ability of their antibodies to
neutralize venom toxins across multiple snake species. This ability results from a production process
involving ...
Immunochemical properties of the N-terminal helix of myotoxin II, a lysine-49 phospholipase A2 from Bothrops asper snake venom
(2001)
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, ...
Antibody-mediated neutralization and binding-reversal studies on α-neurotoxins from micrurus nigrocinctus nigrocinctus (coral snake) venom
(1996-03)
An ELISA based, non-radioactive acetylcholine receptor (AchR) binding assay was used to detect the alpha-neurotoxins present in Micrurus nigrocinctus nigrocinctus venom. Sera from horses hyperimmunized against M. nigrocinctus ...
Inhibition of the myotoxic activity of Bothrops aspermyotoxin II in mice by immunization with its synthetic 13-mer peptide 115-129
(1999)
The region comprising amino acid residues 115±129 of myotoxin II, a Lys49
phospholipase A2 from the venom of Bothrops asper, was previously shown to constitute a
heparin binding site, and to be associated with its toxic ...
Immunochemical and biological characterization of monoclonal antibodies against BaP1, a metalloproteinase from Bothrops asper snake venom
(2010-11)
BaP1 is a P-I class of Snake Venom Metalloproteinase (SVMP) relevant in the local tissue damage associated with envenomations by Bothrops asper, a medically-important species in Central America and parts of South America. ...
Production and partial characterization of monoclonal antibodies to Bothrops asper (terciopelo) myotoxin
(1988)
Seven murine monoclonal antibodies against Bothrops aspen myotoxin were produced and partially characterized. They revealed the presence of at least four cross-reacting basic components in crude venom, with a common subunit ...
Snake venom metalloproteinases: structure/function relationships studies using monoclonal antibodies
(2003-12)
Snake Venom Metalloproteinases (SVMPs) are synthesized as zymogens and undergo proteolytic processing resulting in a variety of multifunctional proteins. Jararhagin is a P-III SVMP, isolated from the venom of Bothrops ...
Immunochemical characterization and role in toxic activities of region 115-129 of myotoxin II, a Lys49 phospholipase A2 from Bothrops asper snake venom
(1998-10)
The region 115–129 of myotoxin II, a catalytically inactive
Lys49 phospholipase A2, was previously shown to
constitute a heparin-binding site and to be involved in
its cytolytic action in vitro. An immunochemical ...