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|Title: ||Purification and characterization of a short insect toxin from the venom of the scorpion Buthus tamulus|
|Authors: ||DHAWAN, R|
|Keywords: ||potassium channels|
|Issue Date: ||2002|
|Publisher: ||ELSEVIER SCIENCE BV|
|Citation: ||FEBS LETTERS, 528(1-3), 261-266|
|Abstract: ||A short chain peptide has been isolated from the venom of a red scorpion of Indian origin, Buthus tamulus. This peptide was purified using ion exchange and reverse phase chromatography and was characterized by molecular weight determination and amino acid sequence. The primary structure analysis shows that BtITx3 is a short peptide of 35 amino acid residues having a molecular weight of 3796 Da. The toxin shows toxicity towards the Lepidopteran species of insect Heli- coverpa armigera causing flaccid paralysis and even death within 24 h. It shows more than 50% homology with the short insectotoxins having four disulfide bridges, which suggests that the toxin belongs to the class of short chain toxins blocking the chloride ion channels. This sequence homology study has also helped to bring out the structure-function relationship between the various short toxins. Homology modeling done by using template structure of a known toxin indicated that this toxin consists of a similar alpha/beta scaffold, as present in other scorpion toxins. (C) 2002 on behalf of the Federation of European Biochemical Societies.|
|Appears in Collections:||Article|
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