Purification of transgenic plant-derived recombinant human acetylcholinesterase-R.

Abstract:

:Nicotiana benthamiana plants were engineered to express a codon-optimized gene encoding the human acetylcholinesterase-R (AChE) isoform. The transgenic plants expressed the protein at >0.4% of total soluble protein, and the plant-produced enzyme was purified to homogeneity. Following lysis, procainamide affinity chromatography and anion-exchange chromatography, more than 400-fold purification was achieved and electrophoretic purity was obtained. This pure protein is kinetically indistinguishable from the only commercially available source of human acetylcholinesterase, which is produced in mammalian cell culture. Thus, we have demonstrated a model system for the production of acetylcholinesterase, which is not susceptible to the quantitative limitations or mammalian pathogens associated with purification from mammalian cell culture or human serum.

journal_name

Chem Biol Interact

authors

Geyer BC,Muralidharan M,Cherni I,Doran J,Fletcher SP,Evron T,Soreq H,Mor TS

doi

10.1016/j.cbi.2005.10.097

subject

Has Abstract

pub_date

2005-12-15 00:00:00

pages

331-4

eissn

0009-2797

issn

1872-7786

pii

S0009-2797(05)00339-X

journal_volume

157-158

pub_type

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