Results 151 to 160 of about 5,580 (197)

Radioiodination of scorpion and snake toxins

Analytical Biochemistry, 1977
Abstract Several scorpion and snake toxins were radioiodinated using the lactoperoxydase method of [125I]iodide oxidation. Two techniques of labeling were set up: (i) Using carrier-free Na125I and 5 μg of toxin, about one iodine atom was incorporated per mole of protein without loss of toxicity.
H, Rochat, M, Tessier, F, Miranda, S, Lissitzky   +3 more
openaire   +2 more sources

The antigenic structure of a scorpion toxin

Molecular Immunology, 1989
Scorpion toxins constitute a family of homologous proteins that exert potent pharmacological effects on ion channels. These proteins are immunogenic and constitute a good model for investigation of the molecular basis of antigenicity. In the first part of this article we summarize the results we have obtained in recent years concerning the location of ...
C, Granier, J, Novotny, J C, Fontecilla-Camps, P, Fourquet, M, el Ayeb, E, Bahraoui   +5 more
openaire   +2 more sources

The insecticidal potential of scorpion β-toxins

Toxicon, 2007
Voltage-gated sodium channels are a major target for toxins and insecticides due to their central role in excitability, but due to the conservation of these channels in Animalia most insecticides do not distinguish between those of insects and mammals, thereby imposing risks to humans and livestock.
Gurevitz, M., Karbat, I., Cohen, L., Ilan, N., Kahn, R., Turkov, M., Stankiewicz, M., Stühmer, W., Dong, K., Gordon, D.   +9 more
openaire   +3 more sources

Interactions of Scorpion Toxins with the Sodium Channel

Annals of the New York Academy of Sciences, 1986
It is evident from the data reviewed that scorpion toxins can be distinguished on the basis of three properties: their effects on Na currents, their specific binding to excitable membranes, and the effects of depolarization and pH on binding and on effect.
H, Meves, J M, Simard, D D, Watt
openaire   +2 more sources

Scorpion toxins prefer salt solutions

Journal of Molecular Modeling, 2015
There is a wide variety of ion channel types with various types of blockers, making research in this field very complicated. To reduce this complexity, it is essential to study ion channels and their blockers independently. Scorpion toxins, a major class of blockers, are charged short peptides with high affinities for potassium channels.
Azadeh, Nikouee, Morteza, Khabiri, Lukasz, Cwiklik   +2 more
openaire   +2 more sources

Conformational variations amongst scorpion toxins

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1986
Circular dichroism spectra were obtained for ten scorpion neurotoxins (representing five species of scorpion) in order to provide an understanding of their relative conformations in solution. Despite a high degree of amino acid sequence homology, the toxins clearly differ from each other in terms of CD-detectable structure.
M J, Dufton, A F, Drake, H, Rochat
openaire   +2 more sources

α-Scorpion toxins

1997
Abstract α-Toxins can be considered as the cause of the scorpion venom toxicity for mammals and particularly human beings, in the ‘Old World’ (Miranda et al. 1970). For example, 90 per cent of the toxicity for the mouse in the venom of Androctonus australis from North Africa is due to only 2 per cent of the weight of the crude venom. The
M -F Martin-Eauclaire, P E Bougis
openaire   +1 more source

[The rational evolution of scorpion toxins].

Bioorganicheskaia khimiia, 1997
A theoretical method for the rational design of a "universal" scorpion toxin with a wider spectrum of specificity for K+ channels and a more stable alpha/beta-folding than in its natural homologues is described. On the basis of the analysis of molecular hydrophobic potentials (MHP) of the protein spatial structures, structural features for a family of ...
Zharavin , V.A., Golovanov, Alexander; id_orcid 0000-0002-8592-3984, Arsen'ev, A. S.   +2 more
openaire   +2 more sources

Full characterization of three toxins from the Androctonus amoreuxi scorpion venom

Toxicon, 2009
In this study, we have characterized the immunological and pharmacological properties of the three major alpha-type toxins from the scorpion Androctonus amoreuxi, AamH1, AamH2 and AamH3, which were previously described as putative toxins from cDNAs [Chen,
Christian Legros, Brigitte Céard, Maya Belghazi   +2 more
exaly   +3 more sources

Enzymes and toxins of the scorpion venom Palamneus gravimanus

Toxicon, 1977
Abstract Hyaluronidase activity (300 units per mg protein) and alkaline phosphatase activity (0.62 × 10-3 units per mg protein) were found in the venom of the scorpion, Palamneus gravimanus. In addition, two toxins have been isolated from the crude venom by gel filtration on Sephadex G-100 and Sephadex G-25, and by isoelectric focusing. The molecular
R P, Wright, T K, Chan, L, Honetschlager, D E, Howell, G V, Odell   +4 more
openaire   +2 more sources