Purification and partial amino acid sequence analysis of human erythrocyte acetylcholinesterase

Vijay Chhajlani, Dwight Derr, Betty Earles, Eli Schmell, Thomas August

Research output: Contribution to journalArticlepeer-review

15 Scopus citations


A single step immunoaffinity purification procedure for human erythrocyte acetylcholinesterase is described which permitted the isolation of milligram quantities of enzyme from 10 U of erythrocytes, with 113 000-fold purification and a yield of about 22%. In SDS-PAGE analysis, the enzyme corresponds to a disulfide linked dimer of 140 kDa which is converted to a 70 kDa monomer upon disulfide reduction. The tryptic peptides generated from purified enzyme were separated by reverse-phase HPLC. Five of these peptides were analysed to determine the amino acid sequences. The obtained sequences showed no homology to the already known amino acid sequences for human serum and brain butyryl-cholinesterase and Torpedo californica acetylcholinesterase.

Original languageEnglish (US)
Pages (from-to)279-282
Number of pages4
JournalFEBS Letters
Issue number2
StatePublished - Apr 24 1989
Externally publishedYes


  • Acetylcholinesterase
  • Amino acid sequence
  • Immunoaffinity chromatography

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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