Purification of transgenic plant-derived recombinant human acetylcholinesterase-R

Brian C. Geyer, Mrinalini Muralidharan, Irene Cherni, Jeffrey Doran, Samuel P. Fletcher, Tama Evron, Hermona Soreq, Tsafrir Leket-Mor

Research output: Contribution to journalArticlepeer-review

25 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)331-334
Number of pages4
JournalChemico-Biological Interactions
StatePublished - Dec 15 2005


  • Acetylcholinesterase
  • Molecular pharming
  • Protein purification
  • Transgenic plants

ASJC Scopus subject areas

  • Toxicology


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