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Mass spectrometry of the human pituitary proteome: identification of selected proteins
Author(s) -
BeranovaGiorgianni Sarka,
Desiderio Dominic M.
Publication year - 2000
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/(sici)1097-0231(20000215)14:3<161::aid-rcm859>3.0.co;2-7
Subject(s) - chemistry , proteome , proteomics , bottom up proteomics , mass spectrometry , trypsin , protein mass spectrometry , chromatography , isobaric labeling , biochemistry , computational biology , electrospray ionization , enzyme , biology , gene
The field of proteomics involves the combined application of advanced separation techniques, mass spectrometry, and bioinformatics tools to characterize proteins in complex biological mixtures. Here we report the identification of nine proteins from the human pituitary proteome, using the proteomics approach. The pituitary proteins were separated by two‐dimensional electrophoresis, and were visualized by silver staining. The proteins of interest were subjected to in‐gel digestion with trypsin, and the masses of the resulting peptides were determined by matrix‐assisted laser desorption/ionization time‐of‐flight mass spectrometry. This tryptic mass map was used to identify the proteins through a search of a protein‐sequence database. The identified proteins include important hormones, and enzymes with various catalytic activities. These proteins will be used to construct a two‐dimensional reference database of the human pituitary. This database will be employed to study changes in the pituitary proteome that are associated with the formation of pituitary tumors. Copyright © 2000 John Wiley & Sons, Ltd.