Enhanced detection of phosphopeptides by MALDI mass spectrometry by use of ammonium sulfate and negative ion detection

Peter S. Backlund, Amina S. Woods, Jinsheng Dong, Alan G. Hennebusch, Alfred L. Yergey

Research output: Chapter in Book/Report/Conference proceedingConference contribution

Abstract

Peptide ionization was analyzed using MALDI mass spectrometry (MS) in the presence of ammonium salts to improve detection of phosphopeptides in peptide mixtures. Standard phosphopeptides from beta-casein and candidate novel phosphopeptides from the yeast protein Gcn2p were identified from MALDI MS by analysis of the relative intensities of positive and negative ions from the peptides. Beta casein were digested with trypsin to generate a peptide mixture containing known phosphopeptides. Ammonium sulfate increased the relative intensity of both phosphopeptides, while ammonium citrate invreased the intensity of phosphopeptide 16-40, but had no effect on phosphopeptide 48-63.

Original languageEnglish (US)
Title of host publicationProceedings 50th ASMS Conference on Mass Spectrometry and Allied Topics
Pages289-290
Number of pages2
StatePublished - 2002
Externally publishedYes
EventProceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics - Orlando, FL, United States
Duration: Jun 2 2002Jun 6 2002

Other

OtherProceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics
CountryUnited States
CityOrlando, FL
Period6/2/026/6/02

ASJC Scopus subject areas

  • Spectroscopy

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