Klukas O, Peshenko I A, Rodionov I L, Teliakova O V, Utkin Iu N, Tsetlin V I
Bioorg Khim. 1995 Feb;21(2):152-5.
Interaction of the mono[125I]iodinated alpha-bungarotoxin and neurotoxin II Naja naja oxiana with the synthetic peptides corresponding to the fragments of the alpha-subunit of nicotinic acetylcholine receptor from Torpedo californica was studied. It was found that both toxins bind to the fragments alpha 186-198, alpha 183-198 and alpha 125-145 adsorbed to the 96-well P.E.T.G. assay plates (COSTAR). Acm-groups on Cys residues did not prevent toxin binding by the peptides studied. Determination of the binding parameters showed that alpha-bungarotoxin interacts with fragment alpha 125-145 less effectively than neurotoxin II. The data obtained demonstrate the presence of different toxin-binding sites on alpha-subunit and confirm the model of multipoint neurotoxin-receptor interaction.
研究了单[¹²⁵I]碘化α-银环蛇毒素和中亚眼镜蛇神经毒素II与对应于加州电鳐烟碱型乙酰胆碱受体α亚基片段的合成肽之间的相互作用。发现这两种毒素都能与吸附在96孔PETG检测板(COSTAR)上的α186 - 198、α183 - 198和α125 - 145片段结合。所研究肽中半胱氨酸残基上的Acm基团并不妨碍毒素与之结合。结合参数的测定表明,α-银环蛇毒素与α125 - 145片段的相互作用比神经毒素II的效果要差。所得数据表明α亚基上存在不同的毒素结合位点,并证实了多点神经毒素-受体相互作用模型。