Yuan_1999_Zhongguo.Yao.Li.Xue.Bao_20_74

AIM: To study the biochemical-pharmacological properties of the recombinant human butyrylcholinesterase (rhBChE) and thereby to size up the potential possibility of using it as a detoxifying agent in succinylcholine intoxication.
METHODS: CHO-dhfr cells were transfected with plasmids by electroporation. BChE activity was 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 expression 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, substrate affinity, inhibitor sensitivity, reactivation, stability, and immunoreactivity with anti-nhBChE antibodies. Mice challenged with 1.5 lethal dose of succinylcholine preincubated with rhBChE survived without any symptoms of intoxication. CONCLUSION: The rhBChE and nhBChE exhibit similar biochemical-pharmacological features. It is of potential value in practical use.