期刊
PROTEOMICS
卷 4, 期 3, 页码 587-598出版社
WILEY
DOI: 10.1002/pmic.200300584
关键词
liquid chromatography-mass spectrometry phosphoprotein; pituitary; post-translational modification
资金
- NCRR NIH HHS [RR 10522, RR 14593] Funding Source: Medline
- NINDS NIH HHS [NS 42843] Funding Source: Medline
Post-translational modifications of proteins from the human pituitary gland play an important role in the regulation of different body functions. We report on the application of a liquid chromatography-tandem mass spectrometry (MS/MS) based approach to detect and characterize phosphorylated proteins in a whole human pituitary digest. By combining an immobilized metal affinity column-based enrichment method with MS/MS conditions that favor the neutral loss of phosphoric acid from a phosphorylated precursor ion, we identified several previously undescribed phosphorylated peptides. The identified peptides were matched to the sequences of six pituitary proteins: the human growth hormone, chromogranin A, secretogranin I, 60S ribosomal protein P1 and/or P2, DnaJ homolog subfamily C member 5, and galanin. The phosphorylation sites of these important regulatory proteins were determined by MS/MS and MS3 analysis.
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