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Identification and characterization of phosphorylated proteins in the human pituitary
Author(s) -
Giorgianni Francesco,
BeranovaGiorgianni Sarka,
Desiderio Dominic M.
Publication year - 2004
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200300584
Subject(s) - chromogranin a , phosphorylation , biochemistry , proteomics , chemistry , tandem mass spectrometry , protein phosphorylation , biology , mass spectrometry , chromatography , protein kinase a , immunohistochemistry , gene , immunology
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 MS 3 analysis.