Improved properties of bovine erythrocyte acetylcholinesterase, isolated by papain cleavage

C. Schmidt-Dannert, H. M. Kalisz, I. Šafařík, R. D. Schmid

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

A simple and rapid procedure involving papain cleavage of the membrane anchor was used to isolate membrane-bound acetylcholinesterase from bovine erythrocytes. The solubilized enzyme was purified 930-fold by ion exchange chromatography and gel filtration. The properties of the papain-cleaved acetylcholinesterase were compared with those of a commercial acetylcholinesterase, solubilized from the erythrocyte membranes by detergents. Cleavage of the membrane anchor eliminated dimer aggregation, caused a pH shift in thermal stability and resulted in increased stability in organic solvents. Bovine serum albumin, used as stabilizer of the commercial enzyme preparation, increased the thermal stability but concomitantly decreased the activity of acetylcholinesterase at pH 6-8. The improved stability of the cleaved acetylcholinesterase, especially in organic solvents, may enhance the biosensor performance of the enzyme.

Original languageEnglish (US)
Pages (from-to)231-237
Number of pages7
JournalJournal of Biotechnology
Volume36
Issue number3
DOIs
StatePublished - Aug 31 1994

Keywords

  • Acetylcholinesterase
  • Bovine erythrocyte
  • Isolation
  • Papain cleavage
  • Stability

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