title: Identification of the trypsin-like activity in commercial preparations of eel acetylcholinesterase.
abstract: 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 trypsin, which is difficult to remove completely during AChE purification.
authors.affiliation: Parke-Davis Pharmaceutical Research Division, Warner-Lambert Company, Department of Pharmacology, Ann Arbor, MI 48106-1047.
authors.forename: R T
authors.initials: RT
authors.lastname: Carroll
authors.forename: M R
authors.initials: MR
authors.lastname: Emmerling
mesh_terms: D000110:Acetylcholinesterase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D004340:Drug Contamination; D004593:Electrophorus; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D012689:Sequence Homology, Nucleic Acid; D013379:Substrate Specificity; D014357:Trypsin / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism
chemical_list: D010446:Peptide Fragments; D000110:Acetylcholinesterase; D014357:Trypsin