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一种针对人乙酰胆碱酯酶的抑制性单克隆抗体。

An inhibitory monoclonal antibody to human acetylcholinesterases.

作者信息

Sorensen K, Brodbeck U, Rasmussen A G, Norgaard-Pedersen B

出版信息

Biochim Biophys Acta. 1987 Mar 18;912(1):56-62. doi: 10.1016/0167-4838(87)90247-0.

Abstract

The monoclonal antibody AE-2 raised against acetylcholinesterase (acetylcholine acetylhydrolase, EC 3.1.1.7) from human erythrocytes is shown to inhibit the enzyme activity. The reaction of the antibody with a structural epitope is investigated further. The epitope resides on monomeric, dimeric and tetrameric species of the enzyme. The rate of phosphorylation of the enzyme by diisopropylfluorophosphate was not affected by the antibody. On the other hand, inhibitors directed towards the anionic site(s) competed with antibody binding, suggesting that one of these is the epitope. The titration with antibody is biphasic and yields about 80% inhibition even in the presence of a large excess of antibody. Inhibition is fully reversible upon dilution, in a time-dependent manner. AE-2 also inhibited human adult and fetal brain acetylcholinesterase (to the same extent). However bovine brain acetylcholinesterase was inhibited to a lesser extent and rat brain acetylcholinesterase did not interact with the antibody. Butyrylcholinesterase (EC 3.1.1.8) also showed no reactivity towards the antibody.

摘要

针对人红细胞乙酰胆碱酯酶(乙酰胆碱乙酰水解酶,EC 3.1.1.7)产生的单克隆抗体AE - 2被证明能抑制该酶的活性。进一步研究了该抗体与一个结构表位的反应。该表位存在于该酶的单体、二聚体和四聚体形式中。二异丙基氟磷酸对该酶的磷酸化速率不受抗体影响。另一方面,针对阴离子位点的抑制剂与抗体结合相互竞争,这表明其中一个阴离子位点就是表位。用抗体进行滴定是双相的,即使在存在大量过量抗体的情况下也能产生约80%的抑制作用。稀释后抑制作用完全可逆,且呈时间依赖性。AE - 2也能抑制成人和胎儿脑乙酰胆碱酯酶(抑制程度相同)。然而,牛脑乙酰胆碱酯酶的抑制程度较小,大鼠脑乙酰胆碱酯酶不与该抗体相互作用。丁酰胆碱酯酶(EC 3.1.1.8)对该抗体也无反应性。

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