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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Journal of bioenergetics and biomembranes 28 (1996), S. 219-230 
    ISSN: 1573-6881
    Keywords: Ion transport ; action potential ; ion channels ; calcium ; sodium ; voltage-dependent gating
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Voltage-gated sodium and calcium channels are responsible for inward movement of sodium and calcium during electrical signals in cell membranes. Their principal subunits are members of a gene family and can function as voltage-gated ion channels by themselves. They are expressed in association with one or more auxiliary subunits which increase functional expression and modify the functional properties of the principal subunits. Structural elements which are required for voltage-dependent activation, selective ion conductance, and inactivation have been identified, and their mechanisms of action are being explored through mutagenesis, expression in heterologous cells, and functional analysis. These experiments reveal that these two channels are built on a common structural theme with variations appropriate for functional specialization of each channel type.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-6830
    Keywords: scorpion toxins ; sodium channel ; ion channels ; electrical excitability
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary 1. A methyl-4-azidobenzimidyl (MAB) derivative of theα-scorpion toxin fromLeiurus quinquestriatus (LqTx) specifically labels only theα subunit of the rat brain sodium channel in synaptosomes or in purified and reconstituted sodium-channel preparations. 2. Unlike previous photoreactive toxin derivatives, binding and photolabeling by MAB-LqTx are allosterically modulated by tetrodotoxin and batrachotoxin, as observed for native LqTx binding to sodium channels in synaptosomes. 3. Proteolytic cleavage of theα subunit photolabeled with MAB-LqTx shows that the label is located within a 60 to 70-kDa protease-resistant core structure in domain I of the sodium-channelα subunit. 4. MAB-LqTx will be valuable in further defining the structure-activity relationships at theα-scorpion toxin receptor site.
    Type of Medium: Electronic Resource
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