Characterization, localization, and biosynthesis of acetylcholinesterase in K 562 cells

Roberto Ravazzolo, Cecilia Garré, Giovanna Bianchi-Scarrá, Renata Barresi, Guido Damiani, Valeria Capra, Franco Ajmar

Research output: Contribution to journalArticlepeer-review


K 562 cell acetylcholinesterase (AChE), identifiable by active site labeling with radioactive diisopropylfluorophosphate (DFP), showed a Mr around 55,000 in both a crude lysate and a purified sample. The K 562 AChE was reactive with one polyclonal and two monoclonal antibodies produced against human erythrocyte AChE. Subcellular localization, investigated by assay on cell fractions, showed that AChE is membrane bound and that it is located on the cell surface as well as on microsomal and Golgi membranes. Biosynthesis of new enzyme molecules, after inactivation of the constitutive AChE with the irreversible inhibitor DFP, allowed us to follow the kinetics of reappearance in the intracellular compartment and at the cell surface (4 and 8 h, respectively).

Original languageEnglish
Pages (from-to)245-251
Number of pages7
JournalArchives of Biochemistry and Biophysics
Issue number1
Publication statusPublished - Nov 15 1988

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


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