一种新型毒素衍生物对纯化及重组钠通道上α-蝎毒素受体位点的光亲和标记
Photoaffinity labeling of the receptor site for alpha-scorpion toxins on purified and reconstituted sodium channels by a new toxin derivative.
作者信息
Tejedor F J, Catterall W A
机构信息
Department of Pharmacology, University of Washington, Seattle 98195.
出版信息
Cell Mol Neurobiol. 1990 Jun;10(2):257-65. doi: 10.1007/BF00734578.
Abstract
- A methyl-4-azidobenzimidyl (MAB) derivative of the alpha-scorpion toxin from Leiurus quinquestriatus (LqTx) specifically labels only the alpha subunit of the rat brain sodium channel in synaptosomes or in purified and reconstituted sodium-channel preparations. 2. Unlike previous photoreactive toxin derivaties, 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 the alpha 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-channel alpha subunit. 4. MAB-LqTx will be valuable in further defining the structure-activity relationships at the alpha-scorpion toxin receptor site.
摘要
- 来自以色列金蝎（Leiurus quinquestriatus）的α-蝎毒素的甲基-4-叠氮基苯并咪唑基（MAB）衍生物（LqTx）仅特异性标记突触体中或纯化及重组的钠通道制剂中的大鼠脑钠通道α亚基。2. 与先前的光反应性毒素衍生物不同，MAB-LqTx的结合和光标记受河豚毒素和蛙毒素的变构调节，这与天然LqTx与突触体中钠通道的结合情况一致。3. 用MAB-LqTx进行光标记的α亚基的蛋白水解切割表明，标记位于钠通道α亚基结构域I中一个60至70 kDa的抗蛋白酶核心结构内。4. MAB-LqTx在进一步确定α-蝎毒素受体位点的构效关系方面将具有重要价值。
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