The proline-rich tetramerization peptides in equine serum butyrylcholinesterase

BİBEROĞLU K., Schopfer L. M., TACAL Ö., Lockridge O.

FEBS JOURNAL, vol.279, no.20, pp.3844-3858, 2012 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 279 Issue: 20
  • Publication Date: 2012
  • Doi Number: 10.1111/j.1742-4658.2012.08744.x
  • Journal Name: FEBS JOURNAL
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.3844-3858
  • Hacettepe University Affiliated: Yes


Soluble, tetrameric, plasma butyrylcholinesterase from horse has previously been shown to include a non-covalently attached polyproline peptide in its structure. The polyproline peptide matched the polyproline-rich region of human lamellipodin. Our goal was to examine the tetramer-organizing peptides of horse butyrylcholinesterase in more detail. Horse butyrylcholinesterase was denatured by boiling, thus releasing a set of polyproline peptides ranging in mass from 1173 to 2098 Da. The peptide sequences were determined by fragmentation in MALDI-TOF-TOF and linear ion trap quadrupole Orbitrap mass spectrometers. Twenty-seven polyproline peptides grouped into 13 families were identified. Peptides contained a minimum of 11 consecutive proline residues and as many as 21. Many of the peptides had a non-proline amino acid at the N-terminus. A search of the protein databanks matched peptides to nine proteins, although not all peptides matched a known protein. It is concluded that polyproline peptides of various lengths and sequences are included in the tetramer structure of horse butyrylcholinesterase. The function of these polyproline peptides is to serve as tetramer-organizing peptides. Structured digital abstract BChE and BChE bind by comigration in non denaturing gel electrophoresis (View interaction) BChE and BChE bind by comigration in sds page (View interaction)