Chiral Recognition of O-Phosphoserine by Mass Spectrometry

Identification and quantification of the enantiomeric excess of O‐phosphoserine (OPSer) residues from post‐translational modified proteins is now possible by the application of a very reproducible and sensitive mass spectrometric method. This technique is based on the different mass‐spectral fragmen...

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Bibliographic Details
Published in:	Angewandte Chemie International Edition Vol. 40; no. 21; pp. 4051 - 4054
Main Authors:	Fago, Giovanna, Filippi, Antonello, Giardini, Anna, Laganà, Aldo, Paladini, Alessandra, Speranza, Maurizio
Format:	Journal Article
Language:	English
Published:	Weinheim WILEY-VCH Verlag GmbH 05-11-2001 WILEY‐VCH Verlag GmbH
Subjects:	chirality enantioselectivity mass spectrometry proteomics enantioselectivity mass spectrometry chirality proteomics
Online Access:	Get full text
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Summary:	Identification and quantification of the enantiomeric excess of O‐phosphoserine (OPSer) residues from post‐translational modified proteins is now possible by the application of a very reproducible and sensitive mass spectrometric method. This technique is based on the different mass‐spectral fragmentation patterns of the diastereomeric cluster ions generated in water/methanol solutions of the analyte (OPSerD/L) with a suitable chiral compound (OPThrL) by collision‐induced dissociation (CID; see mass spectra).
Bibliography:	ark:/67375/WNG-WXJRS1T0-D ArticleID:ANIE4051 istex:8F008DF06E4C97220C94AAFFFE2D0794D409CEB5 This work was supported by the Ministero della Università e della Ricerca Scientifica e Tecnologica (MURST) and the Consiglio Nazionale delle Ricerche (CNR). The authors express their gratitude to F. Angelelli for technical assistance. ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	1433-7851 1521-3773
DOI:	10.1002/1521-3773(20011105)40:21<4051::AID-ANIE4051>3.0.CO;2-4