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首页> 外文期刊>CHROMATOGRAPHY >Enzyme Inhibitory Activity of Ovomucoid Extracted Using a Carboxypeptidase Y-Immobilized Membrane
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Enzyme Inhibitory Activity of Ovomucoid Extracted Using a Carboxypeptidase Y-Immobilized Membrane

机译：羧肽酶Y固定化膜提取的卵类粘液的酶抑制活性

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摘要

Reversible inhibition of enzymes is caused by association and dissociation between enzymes and inhibitors. Therefore, reversible inhibitors can be trapped and extracted using enzyme-inhibitor interaction. The purpose of this study was to establish a method in which the reversible inhibitors retaining the original inhibitory activities are extracted from a single drop of biological sample using the enzyme-inhibitor interaction on the surface of a membrane. A membrane-immobilized carboxypeptidase Y (CPY) was produced after the biotinylated CPY was bound to the avidin separated by nondenaturing electrophoresis, transferred to a polyvinylidene fluoride and stained by Ponceau S. Ovomucoid, possessing reversible CPY inhibitory activity, was trapped and extracted from a single drop of egg white and isolated using the membrane-immobilized CPY. The isolated ovomucoid using this membrane-immobilized CPY possessed a feature that more than 85 % of the relative carboxylesterase activity was suppressed. The results indicate that ovomucoid retaining enzyme inhibitory activities can be isolated from a single drop of egg white sample using enzyme-immobilized membrane.
机译：对酶的可逆抑制是由酶和抑制剂之间的缔合和解离引起的。因此，可逆酶抑制剂可以通过酶-抑制剂相互作用来捕获和提取。这项研究的目的是建立一种方法，其中利用膜表面上的酶-抑制剂相互作用从一滴生物样品中提取保留原始抑制活性的可逆抑制剂。将生物素化的CPY结合到通过非变性电泳分离的抗生物素蛋白上，转移到聚偏二氟乙烯上并用Ponceau S染色后，制得了膜固定的羧肽酶Y（CPY）。捕获具有可逆CPY抑制活性的卵类粘液并从中提取。单滴蛋清，并使用膜固定CPY分离。使用该膜固定化CPY分离的卵类粘液具有以下特征：相对羧酸酯酶活性的85％以上被抑制。结果表明，可以使用固定化酶的膜从一滴蛋清样品中分离出卵类粘液保持酶的抑制活性。

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