Dataset Information

The proline-rich tetramerization peptides in equine serum butyrylcholinesterase.

ABSTRACT: 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.

SUBMITTER: Biberoglu K

PROVIDER: S-EPMC3463765 | biostudies-literature | 2012 Oct

REPOSITORIES: biostudies-literature

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The proline-rich tetramerization peptides in equine serum butyrylcholinesterase.

Biberoglu Kevser K Schopfer Lawrence M LM Tacal Ozden O Lockridge Oksana O

The FEBS journal 20120907 20

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 se ...[more]

PMID: 22889087

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Dataset Information

The proline-rich tetramerization peptides in equine serum butyrylcholinesterase.

Publications

The proline-rich tetramerization peptides in equine serum butyrylcholinesterase.

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