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.
Purification of transgenic plant-derived recombinant human acetylcholinesterase-R
Authors: Geyer BC, Muralidharan M, Cherni I, Doran J, Fletcher SP, Evron T, Soreq H, Mor TS.
Year of publication: 2005
Journal: Chem Biol Interact. 2005 Dec 15;157-158:331-4. Epub 2005 Nov 2.
Link to publication: