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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 ...
Lys-49 phospholipases A2 as active enzymes for beta-arachidonoyl phospholipid bilayer membranes
(1997)
Phospholipases A2 containing Lys-49 have been reported to be extremely weak or
inactive as enzyme. We have recently shown that basic proteins I and II (BP-I and BP-II), Lys-
49-PLA2s isolated from the venom of Trimeresurus ...
Phospholipase A2 myotoxins from Bothrops snake venoms [Artículo de revisión]
(1995-11)
Several myotoxins have been isolated from Bothrops snake venoms during the last 10 years. All of them are group II basic phospholipases A2, although some lack enzymatic activity (i.e. Lys-49 variants). These myotoxins ...
Hyperalgesia induced by Asp49 and Lys49 phospholipases A2 from Bothrops asper snake venom: pharmacological mediation and molecular determinants
(2003-05)
The ability of Lys49 and Asp49 phospholipases A2 (PLA2), from Bothrops asper snake venom, to cause hyperalgesia was investigated in rats, using the paw pressure test. Intraplantar injection of both toxins (5–20 μg/paw) ...
Autocatalytic acylation of phospholipase-like myotoxins
(1995-04)
Several snake venoms contain a phospholipase A2 in which position 49 in the active site is occupied by a lysine or a serine instead of the aspartate residue normally found. Although these proteins do not bind Ca2+ and are ...
Isolation of basic myotoxins from Bothrops Moojeni and Bothrops Atrox snake venoms
(1990)
Three myotoxins, one from the venom of Bothrops atrox and two from the venom of B. moojeni, were isolated by ion-exchange chromatography on CM-Sephadex C-25. The three toxins are basic proteins with an estimated mol. wt ...
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 ...
Activity of hemorrhagic metalloproteinase BaH-1 and myotoxin II from Bothrops asper snake venom on capillary endothelial cells in vitro
(1994-04)
In vivo, hemorrhagic toxins isolated from snake venoms cause a disorganization of the basal lamina of capillaries, with a concomitant degenerative process of endothelial cells. In this study we investigated the effects of ...
Ontogenetic changes in the venom of the snake Lachesis muta stenophrys (bushmaster) from Costa Rica
(1990)
A comparative study was performed on some enzymatic and toxic activities of venoms collected from newborn, one-year old, two-years old and adult (more than five-years old) specimens of Lachesis muta stenophrys. There was ...