Results 111 to 120 of about 686 (159)

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
exaly   +3 more sources

Cytotoxicity of crotoxin on murine erythroleukemia cellsin vitro

Investigational New Drugs, 1993
The cytotoxic effect of crotoxin, a heterodimeric phospholipase A2 from the venom of Crotalus durissus terrificus, was examined on murine erythroleukemia cells in vitro. Crotoxin cytocidal effect on cell growth had an EC50 of approximately 0.1-0.2 microM (3.0-5.0 micrograms/ml) in serum-free medium.
R E, Corin, L J, Viskatis, J C, Vidal, M A, Etcheverry   +3 more
exaly   +3 more sources

Crotoxin acceptor protein isolated from Torpedo electric organ: binding properties to crotoxin by surface plasmon resonance

Toxicon, 2003
Crotoxin, a potent neurotoxin from the South American rattlesnake Crotalus durissus terrificus, is a heterodimeric phospholipase A(2) (EC 3.1.1.4), which blocks the release of acetylcholine from peripheral neurons. We previously have suggested the existence of a 48 kDa crotoxin-binding protein in the presynaptic membranes of the electric organ of ...
Grazyna Fauré, Igor Krizaj
exaly   +3 more sources

Inhibition of crotoxin phospholipase A2 activity by manoalide associated with inactivation of crotoxin toxicity and dissociation of the heterodimeric neurotoxic complex

Biochemical Pharmacology, 2002
Crotoxin (CACB complex) is a convulsant heterodimeric neurotoxic phospholipase A(2) (PLA(2)). The role of phospholipid hydrolysis in its epileptogenic properties remains unresolved. We, thus, studied the effect of manoalide (MLD), a PLA(2) inhibitor, on the toxin catalytic activity and its central and peripheral toxicity.
Frédéric Dorandeu, Grazyna Fauré
exaly   +3 more sources

Biochemistry and pharmacology of the crotoxin complex

Naunyn-Schmiedeberg's Archives of Pharmacology, 1971
K, Rübsamen, H, Breithaupt, E, Habermann   +2 more
exaly   +3 more sources

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

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, R A, Hendon, H, Fraenkel-Conrat   +2 more
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

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

On the subunit structure of crotoxin: Hydrodynamic and shape properties of crotoxin, phospholipase a and crotapotin

Biochemical and Biophysical Research Communications, 1975
Abstract This paper reports physical-chemical properties of the subunit structure of crotoxin, phospholipase A and crotapotin. The native crotoxin has a sedimentation coefficient of 3S and a radius of gyration of Rg = 16.5 A and a molecular weight of 30,900.
H H, Paradies, H, Breithaupt
openaire   +2 more sources