@article{MAKHILLRJBS20116111176,
    title = {Sequence Analysis of Txk from the Scorpion <I>Mesobuthus eupeus</I> Venom Glands Using Semi-Nested RT-PCR},
    journal = {Research Journal of Biological Sciences},
    volume = {6},
    number = {1},
    pages = {12-14},
    year = {2011},
    issn = {1815-8846},
    doi = {rjbsci.2011.12.14},
    url = {https://makhillpublications.co/view-article.php?issn=1815-8846&doi=rjbsci.2011.12.14},
    author = {Ghafar,Abbas and},
    keywords = {amino acid,Armenia,scorpion venom,K+ channels,beta neurotoxin,Sequence analysis},
    abstract = {Natural toxins are useful probes for evaluating the involvement of K+ channels in cell activity and for investigating K+ channel structure and localization. In recent years, peptide toxins that block various K+ channels with high affinity have been purified from diverse animal venoms. One polypeptide beta neurotoxin named Txk was isolated from the venom of scorpion <I>Mesobuthus eupeus</I> of Khuzestan. This toxin consists of 91 amino acid residues which modulate voltage-gated sodium channels gating. In this study, cDNA of Txk &beta;-toxin was amplified and sequence of beta neurotoxin compared with <I>M</I>. <I>martensii occitanus Israelis</I> and <I>Tityus costatus</I> however, the comparison suggests that the length of the peptide is close to the long-chain potassium ion channel blocker peptide family.}
    }