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电鳐乙酰胆碱受体α链天然乙酰胆碱受体肽159 - 169抗原位点的合成

Synthesis of an antigenic site of native acetylcholine receptor peptide 159-169 of Torpedo acetylcholine receptor alpha-chain.

作者信息

McCormick D J, Lennon V A, Atassi M Z

出版信息

Biochem J. 1985 Feb 15;226(1):193-7. doi: 10.1042/bj2260193.

Abstract

A region of the alpha-subunit of the nicotinic acetylcholine receptor (AChR) of the Torpedo electric organ, containing residues 161-166, has been proposed to be a major antigenic site in the native AChR protein. We report the synthesis of a peptide corresponding to residues 159-169, which contains the proposed antigenic region. In quantitative radiometric titrations, radiolabelled anti-(native AChR) antibodies from three different species, rabbit, rat and dog, exhibited considerable binding (approx. 15% relative to native AChR) to Sepharose-immobilized peptide 159-169, but did not bind significantly to Sepharose-immobilized unrelated proteins or peptides. Specificity was further confirmed by the finding that no rabbit anti-AChR antibodies bound to the peptide after absorption with native AChR. These data indicate that the region 159-169 contains an antigenic site that is readily accessible in solubilized native Torpedo AChR.

摘要

电鳐电器官烟碱型乙酰胆碱受体(AChR)α亚基中包含第161 - 166位残基的区域,被认为是天然AChR蛋白中的一个主要抗原位点。我们报道了对应于第159 - 169位残基的肽段的合成,该肽段包含上述抗原区域。在定量放射性滴定中,来自兔、大鼠和犬三种不同物种的放射性标记抗(天然AChR)抗体,与固定在琼脂糖上的肽段159 - 169表现出相当程度的结合(相对于天然AChR约为15%),但与固定在琼脂糖上的无关蛋白质或肽段无明显结合。通过用天然AChR吸收后兔抗AChR抗体不与该肽段结合这一发现,进一步证实了其特异性。这些数据表明,159 - 169区域包含一个在可溶解的天然电鳐AChR中易于接近的抗原位点。

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