Action neuromusculaire comparee de la crotamine et du venin de Crotalus durissus terrificus var. Crotaminicus—II. sur preparations isolees

Cheymol, J; Gonçalves, J.M.; Bourillet, F; Roch-Arveiller, M

doi:10.1016/0041-0101(71)90082-1

Cited by 26 publications

(6 citation statements)

References 2 publications

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“…The supernatant was recovered and injected into a molecular exclusion HPLC column (Superdex 75, 1×60 cm, Pharmacia), previously equilibrated with the same buffer used for dissolving the whole venom. The flow rate used for the elution of the fraction was 0.2 ml/ min; the chromatography was monitored at 280 nm, and the isolated fractions were immediately lyophilized and stored at −10 C. The activities of L-amino acid oxidase (for the identification of gyroxin) and PLA2 (for the identification of crotoxin) were assessed, convulxin was identified according Prado-Franceschi and Brazil (1981), and crotamine was identified according to Cheymol et al (1971).…”

Section: Purification Of Crotalus Durissus Cascavella Venommentioning

confidence: 99%

Comparative studies of the anti-leishmanial activity of three Crotalus durissus ssp. venoms

et al. 2007

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In this study, we compared the anti-leishmanial activity of three crotalic venoms (Crotalus durissus terrificus-Cdt, Crotalus durissus cascavella-Cdca, and Crotalus durissus collilineatus-Cdcol). Different concentrations of each venom incubated with Leishmania (Leishmania) amazonensis promastigotes were used. Cdt venom exhibited a higher anti-leishmanial activity (Inhibitory concentration-IC50-value of 4.70+/-1.72 microg/ml) in comparison with that of Cdca venom (IC50 value of 9.41+/-1.21 microg/ml), while Cdcol venom increased parasite numbers in 50% at a concentration of 44.30+/-2.18 microg/ml. In addition, this venom showed a low anti-leishmanial activity in higher concentrations (IC50 value of 281.00+/-9.50 microg/ml). The main fractions of Cdca venom were isolated and assayed under similar conditions used for assessing crude venom. The most active fractions were gyroxin and crotamine that had IC50 values of 3.80+/-0.52 microg/ml and 19.95+/-4.21 microg/ml, respectively. Convulxin also inhibited parasite growth rate, although this effect was not dose-dependent. Crotoxin was the least effective fraction with an IC50 value of 99.80+/-2.21 microg/ml. None of the protein fractions presented cytotoxic effects against J774 cells in culture. In vivo assays using BALB/c mice revealed that crotoxin and crotamine were the main toxic fractions. In conclusion, C. durissus cascavella venom has three main fractions with anti-leishmanial activity. These results open new possibilities to find proteins that might be used as possible agents against cutaneous leishmaniasis.

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Section: Purification Of Crotalus Durissus Cascavella Venommentioning

confidence: 99%

Comparative studies of the anti-leishmanial activity of three Crotalus durissus ssp. venoms

et al. 2007

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“…The LD 50 values of crotamine reported for mice reveal considerable disparity with a mean of 6,9 mg/kg, varying from 0.07 to 32.76 mg/kg (Moussatche ´et al, 1956;Cheymol et al, 1971;Giglio, 1975;Habermann and Cheng-Raude, 1975; Mebs et al, 1978;Vital-Brazil et al, 1979;Mancin et al, 1998;Boni-Mitake et al, 2001). Such differences could be attributed to the method used in determining LD 50 values, such as type of mice, local of inoculation, solvent of toxin or the injection volume and crotamine purity.…”

Section: Biological Activitymentioning

confidence: 99%

New view on crotamine, a small basic polypeptide myotoxin from South American rattlesnake venom

Oguiura

Boni-Mitake

Rádis‐Baptista

2005

Toxicon

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“…The fraction that elutes in the void volume of the column is nontoxic (Figure 2) and was observed to contain convulxin (Prado-Franceschi & Vital-Brazil, 1969; Vargaftig et al, 1980), a platelet-aggregating glycoprotein (Marlas et al, 1983). The last fraction, which eluted as a polypeptide of apparent Mr of 5000 ± 1000, consisted of a single basic protein which corresponds to crotamine (Laure, 1975): it is toxic when injected intravenously at high doses (DL50 2.3 mg/kg) and possesses the pharmacological properties of this toxin (Cheymol et al, 1971) as tested by C.-C. Chang (personal communication).…”

Section: Crotalus Durissus Terrificus Venommentioning

confidence: 99%

Crotoxin, a phospholipase A2 neurotoxin from the South American rattlesnake Crotalus durissus terrificus: purification of several isoforms and comparison of their molecular structure and of their biological activities

Faure

Bon²

1988

Biochemistry

148

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Crotoxin, the major toxin of the venom of the South American rattlesnake Crotalus durissus terrificus is a mixture of several isoforms that differ slightly in their molecular structure. The toxin consists of two nonidentical subunits: a basic and weakly toxic phospholipase A2, component B, and an acidic and nontoxic subunit, component A. In the present investigation, we have used fast-performance liquid chromatography (FPLC) on anionic and cationic exchange columns to purify isoforms of both crotoxin subunits. Two component A isoforms and four component B isoforms were obtained in a homogeneous state, and their purity was verified by isoelectric focusing in polyacrylamide gels. The amino acid composition of the purified component A and component B isoforms was in good agreement with the protein sequences determined previously with mixtures of isoforms. The amino acid compositions indicated that for both crotoxin components the isoforms differed only by the replacement of few amino acid residues. Eight crotoxin complexes have been prepared in a homogeneous state by reassociation of pure component A and component B isoforms. The quantitative comparison of enzymatic and pharmacological properties of the reconstituted crotoxins indicated that the two component A isoforms had identical properties, whereas the four component B isoforms fell in two classes: crotoxin complexes formed with component B isoforms of the first class were enzymatically less active and pharmacologically more potent than those obtained with component B isoforms of the second class.

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Action neuromusculaire comparee de la crotamine et du venin de Crotalus durissus terrificus var. Crotaminicus—II. sur preparations isolees

Cited by 26 publications

References 2 publications

Comparative studies of the anti-leishmanial activity of three Crotalus durissus ssp. venoms

Comparative studies of the anti-leishmanial activity of three Crotalus durissus ssp. venoms

New view on crotamine, a small basic polypeptide myotoxin from South American rattlesnake venom

Crotoxin, a phospholipase A2 neurotoxin from the South American rattlesnake Crotalus durissus terrificus: purification of several isoforms and comparison of their molecular structure and of their biological activities

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