2002
DOI: 10.1016/s0014-5793(02)03326-4
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Purification and characterization of a short insect toxin from the venom of the scorpion Buthus tamulus

Abstract: A short chain peptide has been isolated from the venom of a red scorpion of Indian origin, Buthus tamulus. This peptide was puri¢ed 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 Helicoverpa armigera causing £accid paralysis and … Show more

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Cited by 20 publications
(6 citation statements)
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“…through a combination of hydrogen bonding, electrostatic, and hydrophobic interactions. 18 However, since the carboxylate terminus of 11-MUA has a net negative charge and chlorotoxin has a net positive charge, 19 it is expected that electrostatic interaction plays a primary role in the CTX adsorption.…”
Section: Resultsmentioning
confidence: 99%
“…through a combination of hydrogen bonding, electrostatic, and hydrophobic interactions. 18 However, since the carboxylate terminus of 11-MUA has a net negative charge and chlorotoxin has a net positive charge, 19 it is expected that electrostatic interaction plays a primary role in the CTX adsorption.…”
Section: Resultsmentioning
confidence: 99%
“…Two known Mesob. tamulus peptides26, 27 (BtITx3, BTK‐2) were represented in the 20 most abundant m/z values detected. These two peptides were present in both sources of venom.…”
Section: Resultsmentioning
confidence: 99%
“…Further, the low molecular weight insect-selective toxins BtTx3 (3,796 Da) and ButaIT (3,856.7 Da) were identified. These toxins can be developed as insecticidal agents against lepidopteran insect species ( Wudayagiri et al, 2001 ; Dhawan et al, 2002 ).…”
Section: Characterization Of Venom and Analyses Of Sequence-structure-functional Impactsmentioning
confidence: 99%