Results 121 to 130 of about 686 (159)

Amino-acid Composition of Crotoxin

Nature, 1951
THE first snake-venom prepared in the pure crystalline form was crotoxin from Crotalus terr. terr. as described in 1938; at that time only its cystine and methionine contents were quantitatively determined1. This protein, with a molecular weight of 30,0002, proved to be homogeneous3 in the ultra-centrifuge2 as well as by electrophoresis4.
K H, SLOTTA, J, PRIMOSIGH
openaire   +2 more sources

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
openaire   +3 more sources

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
openaire   +2 more sources

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
openaire   +2 more sources

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
openaire   +2 more sources

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
openaire   +2 more sources

Investigations on the mechanism of action of crotoxin.

Journal de physiologie, 1985
Crotoxin, the major toxic protein of Crotalus durissus terrificus, is composed of a basic phospholipase, component-B, and of an acidic subunit, component-A. The crotoxin complex is insensitive to an active site directed reagent, p-bromophenacyl bromide, while its isolated enzymatic component-B is rapidly and irreversibly inactivated.
F, Radvanyi, C, Bon
openaire   +2 more sources

Recombinant expression of crotoxin and comparison to native crotoxin as immunogens for anti-crotalid antivenoms

Protein Expression and Purification
The crotoxin complex is identified as the primary lethal toxin in various species of rattlesnakes. It comprises two subunits: CtxA, a non-toxic protein, and CtxB, a minimally toxic enzymatic phospholipase A2. These components exert neurotoxic effects by disrupting neuromuscular transmission, specifically by inhibiting the release of acetylcholine ...
Miguel Angel Mejía Sánchez, Samuel Cardoso Arenas, Ricardo Miranda Blancas, Herlinda Clement, Ligia Luz Corrales García, Adrián Marcelo Franco-Vásquez, Ivan Arenas, Alejandro Carbajal Saucedo, Gerardo Corzo   +8 more
openaire   +2 more sources

Crotoxin

2000
Abstract Crotoxin is a dimeric polypeptide (molecular mass, 23.5 kDa) from the venom of the southern Brazilian rattlesnake (Crotalus durissus terrifi,cus) (8,11). The agent acts pre synaptically at motor nerve terminals. In isolated nerve muscle preparations, its effect on transmitter release occurs in three stages (2): An initial ...
openaire   +1 more source

Induction of tolerance to crotoxin in mice.

The Journal of Pharmacology and Experimental Therapeutics, 1993
Crotoxin, the major toxic component from the venom of Crotalus durissus terrificus is a potent neurotoxin (LD50, i.p., mice, 0.09 mg/kg) which possesses phospholipase A2 activity and causes a blockade of neuromuscular transmission. In this article, we show that mice injected daily with progressively increasing doses of crotoxin develop tolerance to the
M, Okamoto, L J, Viskatis, G, de la Roza, J C, Vidal   +3 more
openaire   +2 more sources