Results 71 to 80 of about 975 (184)

Local tissue damage induced by Bothrops snake venoms - A review [PDF]

open access: yes, 1989
This review focuses on the local effects induced by Bothrops venoms. These envenomation are characterized by myonecrosis, hemorrhage and edema which develop rapidly after venom inoculation.
Lomonte, Bruno, Gutiérrez, José María
core  

Immunohistochemical demonstration of the binding of Bothrops asper myotoxin to skeletal muscle sarcolemma

open access: yesToxicon, 1987
The binding of Bothrops asper myotoxin to mouse skeletal muscle was studied at both the light and electron microscope levels using the peroxidase anti-peroxidase technique. The toxin binds to muscle cell sarcolemma, and there are no intracellular binding sites.
Brenes Pino, Fernando   +2 more
openaire   +4 more sources

South American snake venom proteins antigenically-related to Bothrops asper myotoxins. [PDF]

open access: yes, 1990
the presence of proteins antigenically related to Bothrops asper myotoxins in various snake venoms, mainly from South America, was investigated by using poluclonal and monoclonal antibodies. 2.
Furtado, María de Fátima   +6 more
core  

A Lys49-PLA2 Myotoxin of Bothrops asper triggers a rapid death of macrophages that involves autocrine purinergic receptor signalling [PDF]

open access: yes, 2012
Lys49-PLA(2) myotoxins, an important component of various viperid snake venoms, are a class of PLA(2)-homolog proteins deprived of catalytic activity.
Fernández J.   +22 more
core   +1 more source

Individual expression patterns of myotoxin isoforms in the venom of the snake Bothrops asper

open access: yesComparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1992
1. In order to investigate the distribution of myotoxin isoforms in the snake Bothrops asper, venoms from individual specimens were analyzed by a cathodic electrophoretic system for basic proteins under native conditions. 2. The electrophoretic system resolved at least five bands with slight differences in mobility, corresponding to the fastest ...
Carmona Morera, Elena, Lomonte, Bruno
openaire   +4 more sources

Phospholipases A2 From Viperidae Snake Venoms: How do They Induce Skeletal Muscle Damage? [PDF]

open access: yes, 2011
Phospholipases A2 (PLA2s) are abundant components in snake venoms, which play important toxic roles. This review focuses on group II PLA2s endowed with myotoxic effects, present in Viperidae venoms. These PLA2s are subdivided into catalytically-active (
Lomonte, Bruno, Gutiérrez, José María
core  

Isolation and characterization of basic myotoxic phospholipases A2 from Bothrops godmani (Godman's pit viper) snake venom

open access: yes, 1992
Two basic myotoxic phospholipases A2 were purified to homogeneity from the venom of Bothrops godmani from Costa Rica by ion-exchange chromatography on CM-Sephadex.
Díaz Oreiro, Cecilia   +2 more
core   +1 more source

Immunoenzymatic quantitation of antibodies to Bothrops asper myotoxins after polyvalent antivenom administration in mice. [PDF]

open access: yes, 1992
Two quantitative enzyme-immunoassays (EIA) for Bothrops asper myotoxin and anti-myotoxin antibodies, respectively, were utilized to study their in vivo distribution in mice (Swiss, 18 to 20 g). 2. After polyvalent antivenom (0.4 ml) administration by the
Carmona Morera, Elena   +2 more
core  

Comparative study of synthetic peptides corresponding to region 115-129 in Lys49 myotoxic phospholipases A2 from snake venoms

open access: yes, 2003
Lys49 phospholipase A2 homologues constitute a group of catalytically-inactive proteins, present in the venoms of many crotalid snakes, which induce myonecrosis.
Angulo Ugalde, Yamileth   +2 more
core   +1 more source

Chemical modification of histidine and lysine residues of myotoxic phospholipases A2 isolated from Bothrops asper and Bothrops godmani snake venoms: effects on enzymatic and pharmacological properties

open access: yes, 1997
Lysine and histidine residues of two myotoxic phospholipases A2, Bothrops asper myotoxin III and Bothrops godmani myotoxin I, were chemically modified in order to study the effects of these treatments on enzymatic and pharmacological properties.
Díaz Oreiro, Cecilia   +1 more
core   +1 more source

Home - About - Disclaimer - Privacy