Results 151 to 160 of about 1,959 (214)

Preliminary X-ray crystallographic studies of a tetrameric phospholipase A2 formed by two isoforms of crotoxin B from Crotalus durissus terrificus venom [PDF]

open access: yesActa Crystallographica Section F: Structural Biology Communications, 2007
Crotoxin B is a basic phospholipase A(2) found in the venom of Crotalus durissus terrificus and is one of the subunits that constitute crotoxin. This heterodimeric toxin, which is the main component of C. d.
Guilherme Henrique Marchi Salvador   +2 more
exaly   +2 more sources

Cytotoxic effect of crotoxin on cancer cells and its antitumoral effects correlated to tumor microenvironment: A review.

International Journal of Biological Macromolecules, 2023
Cancer is the second leading cause of death worldwide, and despite the effort of standard treatments, the search for new tools against this disease is necessary.
T. C. Almeida   +5 more
semanticscholar   +1 more source

Synergism of the two subunits of crotoxin

Toxicon, 1982
Crotoxin, a potent neurotoxin from the venom of Crotalus durissus terrificus, is composed of an acidic subunit which is non-toxic and enzymatically inactive and a basic subunit which possesses a phospholipase activity and low toxicity. It is shown that crotoxin very efficiently blocks the cholinergic post-synaptic response of the isolated electroplaque
C Bon
exaly   +3 more sources

Hemodynamic impairment induced by Crotoxin using in vivo and ex vivo approach in a rat model.

International Journal of Biological Macromolecules, 2023
Crotalus durissus snakebite represent 10 % of snakebite cases in Brazil, which cardiovascular disorders are associated with severe cases. Considering crotoxin (CTX) as the major venom component, the present study aimed to evaluate the hemodynamic ...
M. A. Sartim   +7 more
semanticscholar   +1 more source

The mechanism of inhibition of phospholipase activity of crotoxin B by crotoxin A

Toxicon, 1983
In the crotoxin complex isolated from Crotalus durissus terrificus venom, the component A inhibits the phospholipase A2 activity of crotoxin B only when the substrate is in the aggregated form, preventing the interaction of the enzyme with lecithin--water interfaces.
G, Canziani, C, Seki, J C, Vidal
openaire   +2 more sources

Accessibility of the active site of crotoxin B in the crotoxin complex

Toxicon, 1982
Basic phospholipases A and the crotoxin complex isolated from Crotalus durissus terrificus venom exhibited similar initial reaction rates, time course and degree of hydrolysis of synthetic short chain lecithins in the monomeric state. Although monomeric lecithins seem to promote dissociation of crotoxin up to a certain extent, this cannot explain the ...
G, Canziani, C, Seki, J C, Vidal
openaire   +2 more sources

The active components of crotoxin

Biochemical and Biophysical Research Communications, 1972
Summary The main component of Crotalus durissus terrificus venom, crotoxin, represents a natural complex of two types of proteins of isoelectric points at pH 3.7 and 8.6 and molecular weights of about 9000 and 12,000 daltons, respectively. The neurotoxicity of that venom requires the synergistic action of both, while the lecithin requiring ...
J, Horst   +2 more
openaire   +2 more sources

Crotoxin modulates metabolism and secretory activity of peritoneal macrophages from Walker 256 tumor-bearing rats.

Toxicon, 2022
Crotoxin (CTX), the major toxin of Crotalus durissus terrificus snake venom, induces an inhibitory effect on tumor development and modulates the functions of macrophages (MØs), which play a key role as a defense mechanism against tumor growth.
Odair Jorge Faiad   +4 more
semanticscholar   +1 more source

Fractionation and composition of crotoxin

Archives of Biochemistry and Biophysics, 1956
Abstract 1. 1. Crotoxin, upon treatment with fluorodinitrobenzene, yields a water-soluble dinitrophenyl derivative, and a fraction which is insoluble in water and various salt solutions buffered between pH 5 and 10. The latter usually comprises about 65% of the total. 2. 2. The two DNP-proteins differ in their content in most amino acids. The
H, FRAENKEL-CONRAT, B, SINGER
openaire   +2 more sources

Varespladib (LY315920) prevents neuromuscular blockage and myotoxicity induced by crotoxin on mouse neuromuscular preparations.

Toxicon, 2021
Varespladib (LY315920) is a synthetic phospholipase A2 (PLA2) inhibitor that has been demonstrating antiophidic potential against snake venoms that present PLA2 neurotoxins.
Fernanda Valadares Maciel   +6 more
semanticscholar   +1 more source

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