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Primary structure of scorpion anti‐insect toxins isolated from the venom of Leiurus quinquestriatus quinquestriatus
Author(s) -
Kopeyan Charles,
Mansuelle Pascal,
Sampieri François,
Brando Thérèse,
Mostafa Bahraoui El,
Rochat Hervé,
Granier Claude
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80607-k
Subject(s) - venom , scorpion , biology , buthidae , protein primary structure , insect , biochemistry , scorpion venoms , toxin , edman degradation , peptide sequence , zoology , botany , gene
The amino acid sequences of insect‐selective scorpion toxins, purified from the venom of Leiurus quinquestriatus quinquestriatus , have been determined by automatic phenyl isothiocyanate degradation of the S‐carboxymethylated proteins and derived proteolytic peptides. The excitatory toxin Lqq IT 1 and Lqq IT 1 ' (70 residues) show the shift of one half‐cystine from an external position, which is characteristic of anti‐mammal toxins, to an internal sequence position. Lqq IT 2 , (61 residues) displays the half‐cystine residue in position 12, common to the sequence of all known antimammal toxins; it induces flaccid paralysis on insects but is non‐toxic for the mouse. Lqq IT 2 , structurally defines a new type of anti‐insect toxins from scorpion venoms. CD spectra and immunological data are in agreement with this finding.