Abstract
Summary Affinity-purified preparations of acetylcholinesterase (EC 3.1.1.7) from Torpedo californica and Electrophorus electricus were reacted with N-dansylaziridine. The T. californica enzyme was only partially modified under conditions of low ionic strength as a second class of reactive groups became exposed in the presence of Zn 2+ or Cd 2+ . E. electricus enzyme, however, was reactive towards N-dansylaziridine only in the presence of Zn 2+ or Cd 2+ . The modified enzymes were hydrolyzed. Two-dimensional thin layer chromatography of methanol extracts of the hydrolysate from either source revealed the presence of a fluorescent, ninhydrin-positive compound having the same mobility as synthetic dansyl-S-aminoethyl cysteine.
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