Characteristics of recombinant human butyrylcholinesterase

AIM: To study the biochemical-pharmacological properties of the recombinant human butyryl-cholinesterase (rhBChE) and thereby to size up the potential possibility of using it as a detoxifying agent in succinylcholine intoxica tion. METHODS: CHO-dhfr(-) cells were transfected with plasmids by electrop oration. BChE activity Tvas determined colorimetrically by 5, 5'-dithiobis- ( 2-nitrobenzoic acid) (DTNB) method. Antigenicity was estimated by enzyme- linked immunosorbent assay and Western blot. RESULTS: The maximal expressio n amounted to 25.83 ng.h(-1)/10(6) cells. The rhBChE was highly similar to the native human BChE (nhBChE) in terms of its catalytic property, substrat e affinity, inhibitor sensitivity, reactivation, stability, and immunoreact ivity with anti-nhBChE antibodies. Mice challenged with 1.5 lethal dose of succinylcholine preincubated with rhBChE survived without any symptoms of i ntoxication. CONCLUSION: The rhBChE and nhBChE exhibit similar biochemical- pharmacological,features. It is of potential value in practical use.