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dc.contributor.authorBiberoglu, Kevser
dc.contributor.authorSchopfer, Lawrence M.
dc.contributor.authorSaxena, Ashima
dc.contributor.authorTacal, Ozden
dc.contributor.authorLockridge, Oksana
dc.date.accessioned2019-12-16T10:29:33Z
dc.date.available2019-12-16T10:29:33Z
dc.date.issued2013
dc.identifier.issn1570-9639
dc.identifier.urihttps://doi.org/10.1016/j.bbapap.2013.01.009
dc.identifier.urihttp://hdl.handle.net/11655/20138
dc.description.abstractAcetylcholinesterase (AChE) in the serum of fetal cow is a tetramer. The related enzyme, butyrylcholinesterase (BChE), in the sera of humans and horse requires polyproline peptides for assembly into tetramers. Our goal was to determine whether soluble tetrameric AChE includes tetramer organizing peptides in, its structure. Fetal bovine serum AChE was denatured by boiling to release non-covalently bound peptides. Bulk protein was separated from peptides by filtration and by high performance liquid chromatography. Peptide mass and amino acid sequence of the released peptides were determined by MALDI-TOF-TOF and LTQ-Orbitrap mass spectrometry. Twenty polyproline peptides, divided into 5 families, were identified. The longest peptide contained 25 consecutive prolines and no other amino acid. Other polyproline peptides included one non-proline amino acid, for example serine at the C-terminus of 20 prolines. A search of the mammalian proteome database suggested that this assortment of polyproline peptides originated from at least 5 different precursor proteins, none of which were the ColQ or PRiMA of membrane-anchored AChE. To date, AChE and BChE are the only proteins known that include polyproline tetramer organizing peptides in their tetrameric structure. (C) 2013 Elsevier B.V. All rights reserved.
dc.language.isoen
dc.publisherElsevier Science Bv
dc.relation.isversionof10.1016/j.bbapap.2013.01.009
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectBiochemistry & Molecular Biology
dc.subjectBiophysics
dc.titlePolyproline Tetramer Organizing Peptides in Fetal Bovine Serum Acetylcholinesterase
dc.typeinfo:eu-repo/semantics/article
dc.typeinfo:eu-repo/semantics/publishedVersion
dc.relation.journalBiochimica Et Biophysica Acta-Proteins And Proteomics
dc.contributor.departmentBiyokimya
dc.identifier.volume1834
dc.identifier.issue4
dc.identifier.startpage745
dc.identifier.endpage753
dc.description.indexWoS


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