ListarMicrobiología por tema "Reptilian Proteins"
Mostrando ítems 1-10 de 10
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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 ... -
Amino acid sequence of a myotoxic Lys49-phospholipase A2 homologue from the venom of Cerrophidion (Bothrops) godmani
(1998-05-19)The complete amino acid sequence of myotoxin II (godMT-II), a myotoxic phospholipase A2 (PLA2) homologue from the venom of the Central American crotaline snake Cerrophidion (Bothrops) godmani, was determined by direct ... -
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 ... -
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, ... -
Effects of Bothrops asper (terciopelo) myotoxin III, a basic phospholipase A2, on liposomes and mouse gastrocnemius muscle
(1993-02)The action of Bothrops asper myotoxin III, a basic phospholipase A2 which induces acute muscle damage, was studied in mouse gastrocnemius muscle in vivo and in vitro and in multilamellar liposomes. Myonecrosis occurred ... -
Modulation of the Susceptibility of Human Erythrocytes to Snake Venom Myotoxic Phospholipases A2: Role of Negatively Charged Phospholipids as Potential Membrane Binding Sites
(2001-07-01)Cerrophidion (Bothrops) godmani myotoxins I (CGMT-I) and II (CGMT-II), Asp-49 and Lys-49 phospholipases A(2) (PLA2s), which drastically differ in enzymatic activity, were devoid of direct hemolytic effects on erythrocytes ... -
Myotoxin II from Bothrops asper (Terciopelo) venom is a lysine-49 phospholipase A2
(1991)A basic, dimeric myotoxic protein, myotoxin II, purified from Bothrops asper venom has a similar molecular weight and is immunologically cross-reactive with antibodies raised to previously isolated B. asper phospholipases ... -
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 ... -
p-Bromophenacyl bromide modification of Bothrops asper myotoxin II, a lysine-49 phospholipase A2, affects its pharmacological activities
(1993-09)Modification of Bothrops asper myotoxin II, a lysine-49 phospholipase A2 variant, was carried out with p-bromophenacyl bromide. Modified toxin did not show changes in its charge and immunological properties but two of its ... -
Skeletal muscle degeneration and regeneration after injection of bothropstoxin-II, a phospholipase A2 isolated from the venom of the snake Bothrops jararacussu
(1991)A myotoxic phospholipase A2, named bothropstoxin II (BthTX-II), was isolated from the venom of the South American snake Bothrops jararacussu and the pathogenesis of myonecrosis induced by this toxin was studied in mice. ...