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目的：探讨Ｍ受体配基结合位点的分子特点。方法：人工合成ｍ１和ｍ２胆碱受体蛋白在细胞外侧的一段多肽，联接蛋白ＫＬＨ后免疫家兔，制备出抗血清。经ＥＬＩＳＡ法，该抗血清具有效价高和特异性强的特点。观察该抗体对Ｍ受体配基结合位点的影响。结果：特异抗体可影响３Ｈ－ＱＮＢ与Ｍ受体的结合。结论：Ｍ受体的配基结合位点与其细胞外氨基末端的氨基酸序列有关。人工抗原制备高效价特异性Ｍ受体亚型抗体对进一步了解药物与Ｍ受体相互作用的分子机制以及建立新型Ｍ受体的检测方法均有重要意义。
Objective: To investigate the molecular characteristics of M receptor ligand binding sites. Methods: Antisera were prepared by artificial synthesis of m1 and m2 choline receptor protein in the extracellular side of a polypeptide, KLH immunized rabbits. The ELISA method, the antisera with high titer and specificity of the characteristics. The effect of this antibody on the M receptor ligand binding site was observed. Results: Specific antibodies affect the binding of 3H-QNB to M receptors. Conclusion: The ligand binding site of M receptor is related to its extracellular amino terminal amino acid sequence. The preparation of high titer specific M receptor subtype antibodies by artificial antigens is of great importance to further understand the molecular mechanism of drug-M receptor interaction and to establish a new M receptor detection method.