Results 161 to 170 of about 1,795 (192)

Re-examination of crotoxin-membrane interactions

Toxicon, 1996
The interaction of crotoxin with synaptic membranes from Torpedo marmorata has been re-examined, using radioiodinated toxin. In competition experiments, the 'saturable binding' is usually calculated by subtracting the non-saturable binding, determined in the presence of an excess of unlabelled crotoxin, from total binding.
I, Krizaj, G, Faure, F, Gubensek, C, Bon
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Systemic skeletal muscle necrosis induced by crotoxin

Toxicon, 2001
Systemic skeletal muscle necrosis induced by crotoxin, the major component of the venom of Crotalus durissus terrificus, was investigated. Mice received an intramuscular injection of crotoxin (0.35mg/kg body weight) into the right tibialis anterior (TA) muscles, which were evaluated 3h, 24h and 3 days later.
T F, Salvini, A C, Amaral, E H, Miyabara, J A, Turri, P M, Danella, H S, Selistre de Araújo   +5 more
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Inactivation of crotoxin by group-specific reagents

Biochimica et Biophysica Acta, 1950
Acetylation of most of the amino groups, or esterification of the carboxyl groups of crotoxin causes extensive detoxication. Sulfation of the aliphatic hydroxyl groups, or iodination of most of the phenolic groups, or coupling of these and imidazole groups of the rattlesnake neurotoxin also causes inactivation.
H, FRAENKEL-CONRAT, J, FRAENKEL-CONRAT
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Influence of temperature upon effects of crotoxin and gamma-irradiated crotoxin at rat neuromuscular transmission

Toxicology Letters, 2000
The influence of temperature upon the effects of crotoxin (CTX), from Crotalus durissus terrificus venom, and gamma-irradiated (60Co, 2000 Gy) crotoxin (iCTX) was studied in rat neuromuscular transmission 'in vitro'. Indirect twitches were evoked in the phrenic-diaphragm preparation by supramaximal strength pulses with a duration of 0.5 ms and ...
Gallacci, M., Nascimento, N., Rogero, JR, Vassilieff, V. S.   +3 more
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Preparation of a crotoxin neutralizing monoclonal antibody

Toxicon, 1988
Crotoxin is a heterodimeric protein composed of an acidic and basic subunit from the venom of Crotalus durissus terrificus and is representative of a number of presynaptically acting neurotoxins found in the venom of rattlesnakes. Four different monoclonal antibodies, typed as IgG1 subclass, were raised against the basic subunit of this toxin.
I I, Kaiser, J L, Middlebrook
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Activation of crotoxin B by volvatoxin A2

Biochemical and Biophysical Research Communications, 1976
Abstract Of the two proteins making up volvatoxin, a mushroom toxin, the smaller, volvatoxin A2, of molecular weight 25,000, is able to synergistically increase the low neurotoxicity of crotoxin B, the larger basic component of the Crotalus durissus terrificus neurotoxin, crotoxin.
T W, Jeng, H, Fraenkel-Conrat
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Crotoxin induces aggregation of human washed platelets

Toxicon, 1994
Crotoxin, the main toxic component isolated from the venom of the South American rattlesnake Crotalus durissus terrificus, is a reversible protein complex composed of a non-toxic non-enzymatic acidic polypeptide (crotapotin) and a toxic basic phospholipase A2 (PLA2).
E C, Landucci, A, Condino-Neto, A C, Perez, S, Hyslop, A P, Corrado, J C, Novello, S, Marangoni, B, Oliveira, E, Antunes, G, de Nucci   +9 more
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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, Faure, Alenka, Copic, Sabine, Le Porrier, Franc, Gubensek, Cassian, Bon, Igor, Krizaj   +5 more
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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
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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
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