Mulac-Jericevic B, Atassi M Z
Marrs McLean Department of Biochemistry, Baylor College of Medicine, Houston, TX 77030.
Biochem J. 1987 Dec 15;248(3):847-52. doi: 10.1042/bj2480847.
The continuous alpha-neurotoxin-binding regions on the extracellular part (residues 1-210) of the alpha-chain of Torpedo californica acetylcholine receptor were localized by reaction of 125I-labelled alpha-bungarotoxin with synthetic overlapping peptides spanning this entire part of the chain. The specificity of the binding was confirmed by inhibition with unlabelled toxin and, for appropriate peptides, with unlabelled anti-(acetylcholine receptor) antibodies. Five toxin-binding regions were localized within residues 1-10, 32-41, 100-115, 122-150 and 182-198. The third, fourth and fifth (and to a lesser extent the first and second) toxin-binding regions overlapped with regions recognized by anti-(acetylcholine receptor) antibodies. The five toxin-binding regions may be distinct sites or, alternatively, different 'faces' in one (or more) sites.
通过用¹²⁵I标记的α-银环蛇毒素与跨越该链这一整个部分的合成重叠肽反应,定位了加州电鳐乙酰胆碱受体α链细胞外部分(第1至210位氨基酸残基)上连续的α-神经毒素结合区域。用未标记的毒素以及对于合适的肽用未标记的抗(乙酰胆碱受体)抗体进行抑制,证实了结合的特异性。五个毒素结合区域定位于第1至10、32至41、100至115、122至150和182至198位氨基酸残基内。第三、第四和第五(以及在较小程度上第一和第二)毒素结合区域与抗(乙酰胆碱受体)抗体识别的区域重叠。这五个毒素结合区域可能是不同的位点,或者是一个(或多个)位点中的不同“面”。