Results 161 to 170 of about 5,580 (197)
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Tityus serrulatus Scorpion Venom and Toxins: An Overview
Protein & Peptide Letters, 2009Tityus serrulatus is considered the most dangerous scorpion in South America and responsible for most of the fatal cases. This review will focus on Tityus serrulatus scorpion venom (Tsv), its long-chain Na(+)-channel toxins (NaTx), which include alpha- and beta-neurotoxins, short-chain K(+)-channel toxins (KTx), hyaluronidase, proteases and other ...
Cologna, Camila T. +4 more
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Scorpion Toxin Polyptides as Therapeutic Agents: An Overview
Protein & Peptide Letters, 2016Scorpions are distributed throughout the world and numerous biological molecules are found in their venom most importantly peptide toxins. These toxins modulate the ion channels either by blocking the pore of the channel or by altering the voltage gating. Molecules which block the pores have been useful in deciphering the structure of the ion channels.
Janardhan, Bhavya +3 more
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Physiological Action of the Toxin of the Egyptian Scorpion
Nature, 1950THE main physiological effects produced by the toxin of the Egyptian scorpion1 are: (1) inhibition of rabbit smooth muscle; (2) acceleration of the isolated rabbit and frog heart (antagonized by ergotoxin); (3) rise of blood pressure of the dog (reversed by ergotoxin); (4) vomiting, and contraction of intestine and bladder of rabbit and dog in the ...
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Respiratory arrhythmias produced by purified scorpion toxin
Toxicon, 1973Abstract Bilateral section of vagi nerves and denervation of carotid bodies prevented the gasping, ataxic and periodic respirations produced by purified scorpion toxin ( Tityus serrulatus ) in the rat. The apnea recorded in intact rats after toxin injection was of long duration in comparison with that observed in denervated animals.
L, Freire-Maia +2 more
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1997
Abstract β-Toxins are responsible for the life hazard constituted, in Central and South America, by scorpion stings. They are qualitatively and quantitatively the most important polypeptides of the venom. They are made of one single polypeptide chain of 60 to 66 amino acid residues crosslinked by four disulfide bridges (Possani et al ...
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Abstract β-Toxins are responsible for the life hazard constituted, in Central and South America, by scorpion stings. They are qualitatively and quantitatively the most important polypeptides of the venom. They are made of one single polypeptide chain of 60 to 66 amino acid residues crosslinked by four disulfide bridges (Possani et al ...
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Scorpion Toxins Affecting Insects
1992Publisher Summary This chapter provides an overview of the scorpion toxins affecting insects. The scorpion toxins specific for insects are divided into two different categories—contraction-inducing toxins, which causes rapid excitatory contraction paralysis in Sarcophaga argyrostoma fly larvae, and depressant toxins, which induces a slow depressant ...
Erwann P. Loret +4 more
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Immunological Properties of Scorpion Toxins
2000Early studies on scorpion venom were motivated by the problems of treating envenomation in various parts of the world (Goyffon et al.,1982; Freire-Maia et al.,1994; Dehesa-Davila et al., 1994). Over the last 30 years, there has been extensive work by our groups and others to elucidate the mechanism of envenomation and to fight against the noxious ...
Christiane Devaux, Mohamed El Ayeb
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Scorpion toxins: Tools for studying K+ channels
Toxicon, 1998Over the last period of time, a large number of scorpion toxins have been characterized. These peptidyl inhibitors of K+ channels have been very useful as probes for determining the molecular architecture of these channels, for purifying channels from native tissue and determining their subunit composition, for developing the pharmacology of K ...
M L, Garcia, M, Hanner, G J, Kaczorowski
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Pharmacology of scorpion toxin II in the skeletal muscle
Naunyn-Schmiedeberg's Archives of Pharmacology, 19751. Scorpion toxin II is potent in inducing contracture and spontaneous contractions of the chick biventer cervicis muscle. In addition, this toxin induces membrane depolarization and blockade of neuromuscular transmission in this muscle preparation. The purpose of the present study is to explore the possible mechanism of actions of toxin II. 2.
S S, Lin, W C, Tseng, C Y, Lee
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Binding of .beta.-scorpion toxin: a physicochemical study
Biochemistry, 1984The binding to rat brain synaptosomes of a beta-scorpion toxin, i.e., toxin II of Centruroides suffusus suffusus (Css II), was studied as a function of pH, temperature, and concentration of some monovalent and divalent cations. At 10 degrees C and pH 6.0, the specific binding of 125I-labeled Css II corresponds to a single class of noninteracting high ...
E, Jover, J, Bablito, F, Couraud
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