PURIFICATION OF THE SAXITOXIN RECEPTOR OF THE SODIUM-CHANNEL FROM RAT-BRAIN
PURIFICATION OF THE SAXITOXIN RECEPTOR OF THE SODIUM-CHANNEL FROM RAT-BRAIN
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DOI：
10.1073/pnas.78.7.4620
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发表时间：
1981-01-01
期刊：
影响因子：
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通讯作者：
CATTERALL, WA
中科院分区：
文献类型：
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作者：
HARTSHORNE, RP;CATTERALL, WA
石房蛤毒素（STX）受体纯化740倍，从大鼠脑通过离子交换层析，麦胚凝集素层析和沉淀在蔗糖梯度上的比活性为1488 pmol/mg的蛋白质。最好的馏分，估计是47%的纯度，从他们的比活性或66%的纯度的基础上NaDodSO 4凝胶电泳。两种多肽，α. (MW. apprxeq.二十七万。10，000）和β。(MW. apprxeq.三万八千三百。2000年）（平均值±。SD）与STX结合活性共纯化。具有相同表观MW的两种多肽在大鼠脑突触体中被125 I标记的蝎毒素的光反应性衍生物特异性地共价标记，并且可能与α相同。和β溶解的STX受体具有316，000 ±的MW。63，000，将其组成限制为1 α。多肽和1个或多个β多肽。每个可溶性受体的多肽。α和β多肽可能含有STX结合位点和哺乳动物Na+通道的蝎毒素结合位点。
The saxitoxin (STX) receptor was purified 740-fold from rat brain by a combination of ion exchange chromatography, wheat germ agglutinin chromatography and sedimentation on sucrose gradients to a specific activity of 1488 pmol/mg of protein. The best fractions were estimated to be 47% pure from their specific activity or 66% pure on the basis of NaDodSO4 gel electrophoresis. Two polypeptides, .alpha. (MW .apprxeq. 270,000 .+-. 10,000) and .beta. (MW .apprxeq. 38,300 .+-. 2000) (mean .+-. SD) copurify with STX binding activity. Two polypeptides of the same apparent MW are specifically covalently labeled by photoreactive derivatives of 125I-labeled scorpion toxin in rat brain synaptosomes and are likely to be identical to .alpha. and .beta.. The solubilized STX receptor has a MW of 316,000 .+-. 63,000, limiting its composition to 1 .alpha. polypeptide and 1 or more .beta. polypeptides per soluble receptor. The .alpha. and .beta. polypeptides probably contain both the STX binding site and the scorpion toxin binding site of the mammalian Na+ channel.