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机构地区:[1]军事医学科学院毒物药物研究所 [2]微生物与流行病研究所
出 处:《中国药理学报》1994年第3期193-196,共4页Acta Pharmacologica Sinica
基 金:Project supported by the National Natural Science Foundation of China,№ 38970211.
摘 要:电器官还原并烷化的乙酰胆碱酯酶(RA-A ChE)的溴化氰裂解肽或又经胃蛋白酶切割的肽与抗RA-AChE单克隆抗体E9、F6及F12仍有抗原抗体反应。经溴化氰及胰蛋白酶割的肽与3者反应消失。氧化破坏RA-AChE糖侧链、溴化氰裂解的RA-A ChE又经酶切除糖侧链后,与3者反应无变化。E9、F6及F12所识别的抗原决定簇是多肽型,不是多糖型。Peptides of the reduced and alkylated acetylcholinesterase (RA-AChE) from the electric organ of Torpediniformes Torpedo torpedo subjected to bromo-cynogen (CNBr) cleavage or/and peptic digestion con-served well the antigen-antibody reactivity with anti-RA-AChE ?monoclonal antibodies E9, F6, and F12, whereas peptides produced by CNBr and tryptic treatments lost all the reactivity. Periodate oxidation of the RA-AChE or glycopeptidase digestion of the CNBr cleaved RA-AChE did not change the antigen-antibody reactivity. It implied that the epi-topes recognized by the 3 anti-RA-AChE monoclonal antibodies are all peptide determinants rather than carbohydrate determinants.
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