Purified omega-conotoxin GVIA receptor of rat brain resembles a dihydropyridine-sensitive L-type calcium channel.
Purified omega-conotoxin GVIA receptor of rat brain resembles a dihydropyridine-sensitive L-type calcium channel.
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大鼠脑中纯化的 omega-芋螺毒素 GVIA 受体类似于二氢吡啶敏感的 L 型钙通道。
DOI：
10.1073/pnas.88.24.11095
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发表时间：
1991
影响因子：
11.1
通讯作者：
Snyder,SH
中科院分区：
文献类型：
--
作者：
McEnery,MW;Snowman,AM;Sharp,AH;Adams,ME;Snyder,SH
通过监测125i标记的CTX （125I-CTX）的可逆结合和n -羟基琥珀酰酰-4-叠氮苯甲酯-125I-CTX （HSA-125I-CTX）的光结合，omega- concontoxin GVIA （CTX）受体被纯化了1900倍，达到明显的均匀性。HSA-125I-CTX光结合到230-kDa蛋白中的药理学和色谱图谱表明，230-kDa蛋白是受体的ctx结合亚基。125I-CTX与纯化的CTX受体结合的药理学特异性与天然膜结合形式对CTX （Kd = 32 pM）和其他肽毒素拮抗剂的敏感性非常相似。纯化的CTX受体包括230 kDa蛋白（α 1）和另外四个表观分子质量分别为140 （α 2）、110、70 （β 2）和60 (β 1) kDa的蛋白。这种亚基结构与1,4-二氢吡啶敏感的l型钙通道非常相似。
The omega-conotoxin GVIA (CTX) receptor has been purified 1900-fold to apparent homogeneity by monitoring both reversible binding of 125I-labeled CTX (125I-CTX) and photoincorporation of N-hydroxysuccinimidyl-4-azidobenzoate-125I-CTX (HSA-125I-CTX). Photoincorporation of HSA-125I-CTX into a 230-kDa protein exhibits a pharmacologic and chromatographic profile indicating that the 230-kDa protein is the CTX-binding subunit of the receptor. The pharmacologic specificity of 125I-CTX binding to the purified CTX receptor closely resembles that of the native membrane-bound form with respect to sensitivity towards CTX (Kd = 32 pM) and other peptide toxin antagonists. The purified CTX receptor comprises the 230-kDa protein (alpha 1) and four additional proteins with apparent molecular masses of 140 (alpha 2), 110, 70 (beta 2), and 60 (beta 1) kDa. This subunit structure closely resembles that of the 1,4-dihydropyridine-sensitive L-type calcium channel.