Author:
Ilyushin D. G.,Haertley O. M.,Bobik T. V.,Shamborant O. G.,Surina E. A.,Knorre V. D.,Masson P.,Smirnov I. V.,Gabibov A. G.,Ponomarenko N. A.
Abstract
Butyrylcholinesterase (BChE) is a serine hydrolase (EC 3.1.1.8) which can be found in most animal tissues. This enzyme has a broad spectrum of efficacy against organophosphorus compounds, which makes it a prime candidate for the role of stoichiometric bioscavenger. Development of a new-age DNA-encoded bioscavenger is a vival task. Several transgenic expression systems of human BChE were developed over the past 20 years; however, none of them has been shown to make economic sense or has been approved for administration to humans. In this study, a CHO-based expression system was redesigned, resulting in a significant increase in the production level of functional recombinant human butyrylcholinesterase as compared to the hitherto existing systems. The recombinant enzyme was characterized with Elman and ELISA methods.
Subject
Molecular Biology,Molecular Medicine,Biochemistry,Biotechnology
Cited by
20 articles.
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