Susceptibility of the hydroxyl groups in serine and threonine to β-elimination/Michael addition under commonly used moderately high-temperature conditions

Analytical Biochemistry

Volumn 323, Issue 1, 2003, Pages 94-102

  Li, Wei ^a   Backlund, Peter S ^a   Boykins, Robert A ^b   Wang, Guiyu ^a   Chen, Hao Chia ^a  

^a EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH AND HUMAN DEVELOPMENT   (United States)

^b Division of Viral Products   (United States)

Author keywords

LC MS MS; MALDI TOF; Phosphopeptide; Phosphoserine; Phosphothreonine; Elimination Michael addition reaction

Indexed keywords

ADDITION REACTIONS; ELECTROSPRAY IONIZATION; MASS SPECTROMETERS; MASS SPECTROMETRY; PHOSPHORYLATION; POSITIVE IONS; SODIUM HYDROXIDE; SODIUM SULFITE;

LC-MS/MS; MALDI-TOF; PHOSPHOPEPTIDES; PHOSPHOSERINE; PHOSPHOTHREONINE;

AMINO ACIDS;

HYDROXYL GROUP; PHOSPHOPEPTIDE; SERINE; SODIUM HYDROXIDE; THIOL DERIVATIVE; THREONINE;

ALKALINITY; ARTICLE; BETA ELIMINATION; CHEMICAL MODIFICATION; CHEMICAL REACTION; HIGH TEMPERATURE; MASS SPECTROMETRY; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; MICHAEL ADDITION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN LOCALIZATION; TANDEM MASS SPECTROMETRY;

EID: 0242690399     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ab.2003.08.015     Document Type: Article

References (27)

1. Hunter T. Signaling and beyond. Cell. 100:2000;113-127.
2. McLachlin D.T., Chait B.T. Analysis of phosphorylated proteins and peptides by mass spectrometry. Curr. Opin. Chem. Biol. 5:2001;591-602.
3. Mann M., Hendrickson R.C., Pandey A. Analysis of proteins and proteomes by mass spectrometry. Annu. Rev. Biochem. 70:2001;437-473.
4. Degnore J.P., Qin J. Fragmentation of phosphopeptides in an ion trap mass spectrometer. J. Am. Soc. Mass Spectrom. 9:1998;1175-1188.
5. Sickmann A., Meyer H.E. Phosphoamino acid analysis. Proteomics. 1:2001;200-206.
6. Stensballe A., Andersen S., Jensen O.N. Characterization of phosphoproteins from electrophoretic gels by nanoscale Fe(III) affinity chromatography with off-line mass spectrometry analysis. Proteomics. 1:2001;207-222.
7. Steen H., Mann M. A new derivatization strategy for the analysis of phosphopeptides by precursor ion scanning in positive ion mode. J. Am. Soc. Mass Spectrom. 13:2002;996-1003.
8. Jaffe H., Veeranna H., Pant H.C. Characterization of serine and threonine phosphorylation sites in. β -elimination/ethanethiol addition-modified proteins by electrospray tandem mass spectrometry and database searching Biochemistry. 37:1998;16211-16224.
9. Li W., Boykins R.A., Backlund P.S., Wang G.Y., Chen H.-C. Identification of phosphoserine and phosphothreonine as cysteic acid and. β -methylcysteic acid residues in peptides by tandem mass spectrometric sequencing Anal. Chem. 74:2002;5701-5710.
10. Resing K.A., Johnson R.S., Walsh K.A. Mass spectrometric analysis of 21 phosphorylation sites in the internal repeat of rat profilaggrin, precursor of an intermediate filament associated protein. Biochemistry. 34:1995;9477-9487.
11. Weckwerth W., Willmitzer L., Fiehn O. Comparative quantification and identification of phosphoproteins using stable isotope labeling and liquid chromatography/mass spectrometry. Rapid. Commun. Mass Spectrom. 14:2000;1677-1681.
12. Oda Y., Nagasu T., Chait B.T. Enrichment, Analysis of Phosphorylated proteins as a tool for probing the phosphoproteome. Nat. Biotechnol. 19:2001;379-382.
13. Goshe M.B., Conrads T.P., Panisko E.A., Angell N.H., Veenstra T.D., Smith R.D. Phosphoprotein isotope-coded affinity tag approach for isolating and quantitating phosphopeptides in proteome-wide analyses. Anal. Chem. 73:2001;2578-2586.
14. Molloy M.P., Andrews P.C. Phosphopeptide derivatization signatures to identify serine and threonine phosphorylated peptides by mass spectrometry. Anal. Chem. 73:2001;5387-5394.
15. Aitken A., Howell S., Jones D., Madrazo J., Patel Y. 14-3-3. α and δ are the phosphorylated forms of Raf-activating 14-3-3 β and ζ J. Biol. Chem. 270:1995;5706-5709.
16. Lapko V.N., Jiang X.Y., Smith D.L., Song P.S. Posttranslational modification of specific serine in a multiple serine cluster. Biochemistry. 36:1997;10595-10599.
17. Simpson D.L., Hranisavljevic J., Davidson E.A. β -Elimination and sulfite addition as means of localization and identification of substituted seryl and threonyl residues in proteins and proteoglycans Biochemistry. 11:1972;1849-1856.
18. Kolesnikova V.Y., Sklyankina V.A., Baratova L.A., Nazarova T.I., Avaeva S.M. Modification of O-phosphoserine residues in phosphoproteins. Biochhimiya. 39:1974;235-240. (English translation).
19. Isemura M., Ikenaka T. β -Elimination and sulfite addition reaction of chondroitin sulfate peptidoglycan and the peptide structure of the linkage region Biochim. Biophys. Acta. 401:1975;11-21.
20. Downs F., Peterson C., Murty V.L.N., Pigman W. Quantitation of. β -elimination reaction as used on glycoproteins Int. J. Pep. Protein Res. 10:1977;315-322.
21. Clark R.C. Chemical modification of phosvitin: methylmercaptovitin; The fate of phosphothreonine and its significance with respect to sequence analysis. Int. J. Biochem. 13:1981;233-236.
22. Clark R.C., Dijkstra J. Chemical modification of phosvitin: preparation of dimethylaminovitin and methylmercaptovitin and their utility for elucidation of phosvitin primary structure. Int. J. Biochem. 11:1980;577-585.
23. Annan W.D., Manson W., Nimmo J.A. The identification of phosphoseryl residues during determination of amino acid sequence in phosphoproteins. Anal. Biochem. 121:1982;62-68.
24. Mega T., Hamazume Y., Hong Y.M., Ikenaka T., Nong Y.M. Studies on the methods for the determination of phosphorylation sites in highly phosphorylated peptides or proteins: phosphorylation sites of hen egg white riboflavin binding protein. J. Biochem. 100:1986;1109-1116.
25. Meyer H.E., Hoffmann-Posorske E., Korte H., Heilmeyer L.M.G. Sequence analysis of phosphoserine containing peptides. Modification for picomolar sensitivity. FEBS Lett. 204:1986;61-66.
26. Mega T., Nakamura N., Ikenaka T. Modification of substituted seryl and threonyl residues in phosphopeptides and polysialoglycoprotein by. β -elimination and nucleophile additions J. Biochem. 107:1990;68-72.
27. Aitken A., Learmonth M. Analysis of site of protein phosphorylation. Methods in Molecular Biology, Protein Sequencing Protocols. 64:1997;293-306 Humana press Inc, Totowa.