Identification of the trypsin-like activity in commercial preparations of eel acetylcholinesterase.

@article{Carroll1991IdentificationOT,
  title={Identification of the trypsin-like activity in commercial preparations of eel acetylcholinesterase.},
  author={Rebecka T Carroll and Mark R. Emmerling},
  journal={Biochemical and biophysical research communications},
  year={1991},
  volume={181 2},
  pages={858-62}
}
Electricus electrophorus acetylcholinesterase (AChE, EC 3.1.1.7) is reported to possess a trypsin-like activity. We found that purification of AChE removes over 99% of this protease activity, which resides in a single 25 kDa protein with an N-terminal sequence identical to bovine pancreatic trypsin. Digests of neuropeptides using purified eel AChE or bovine pancreatic trypsin gave identical peptide maps. These results indicate that the commercial preparation of eel AChE is contaminated by a… CONTINUE READING

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