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  • 1
    Digitale Medien
    Digitale Medien
    Springer
    Journal of bioenergetics and biomembranes 28 (1996), S. 219-230 
    ISSN: 1573-6881
    Schlagwort(e): Ion transport ; action potential ; ion channels ; calcium ; sodium ; voltage-dependent gating
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie , Physik
    Notizen: 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.
    Materialart: Digitale Medien
    Standort Signatur Einschränkungen Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Springer
    Cellular and molecular neurobiology 10 (1990), S. 257-265 
    ISSN: 1573-6830
    Schlagwort(e): scorpion toxins ; sodium channel ; ion channels ; electrical excitability
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: 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.
    Materialart: Digitale Medien
    Standort Signatur Einschränkungen Verfügbarkeit
    BibTip Andere fanden auch interessant ...
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