Donnelly-Roberts D L, Lentz T L
Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06510.
Biochem Biophys Res Commun. 1989 Apr 14;160(1):289-95. doi: 10.1016/0006-291x(89)91654-9.
Polyclonal and monoclonal antibodies were raised against a peptide comprising residues 173-204 of the alpha-subunit of the acetylcholine receptor. The polyclonal and pooled monoclonal antibodies inhibited up to 50% of 125I-alpha-bungarotoxin binding to peptide 173-204. Some of the antibodies recognized native receptor but did not significantly affect alpha-bungarotoxin binding. Epitope mapping revealed that the antibodies are directed against residues 183-194 indicating this region is a major determinant of toxin binding. This region is most likely conformationally constrained in the native receptor.
制备了针对乙酰胆碱受体α亚基173 - 204位残基组成的肽段的多克隆抗体和单克隆抗体。多克隆抗体和混合单克隆抗体可抑制高达50%的125I-α-银环蛇毒素与173 - 204肽段的结合。一些抗体识别天然受体，但对α-银环蛇毒素的结合没有显著影响。表位作图显示这些抗体针对的是183 - 194位残基，表明该区域是毒素结合的主要决定因素。该区域在天然受体中很可能受到构象限制。
