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Proteome analysis in the bovine adrenal medulla using liquid chromatography with tandem mass spectrometry
Author(s) -
Jalili Pegah R.,
Dass Chhabil
Publication year - 2004
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/rcm.1564
Subject(s) - chemistry , chromatography , mass spectrometry , tandem mass spectrometry , high performance liquid chromatography , liquid chromatography–mass spectrometry , proteome , proteomics , adrenal medulla , biochemistry , medicine , catecholamine , gene
Liquid chromatography/mass spectrometry (LC/MS)‐based proteomics has been used to identify soluble proteins in the bovine adrenal medulla. This gland is a major source of hormones, opioids, neurotransmitters, and several vital proteins. The adrenal medulla proteins were first purified using ammonium sulfate precipitation. The resulting proteins were then pre‐fractionated with a C‐4 high‐peformance liquid chromatography (HPLC) column. Each 2‐min HPLC fraction was digested with trypsin, and separated further and analyzed using capillary liquid chromatography/tandem mass spectrometry (capLC/nanospray‐MS/MS) to map the proteome of the adrenal medulla. The parent mass and sequence ion information thus obtained for tryptic peptides was used to search the NCBInr database using the SEQUEST search engine. A total of 195 proteins were identified, of which 71 had good scores (delta correlation value greater than 0.1, preliminary score above 200, and cross‐correlation value above 2.5). The prominent proteins thus identified are secretogranin I precursor, chromogranin A, proenkephalin A precursor, myosin X, hemoglobin beta chain, hemoglobin alpha chain, heat shock protein 10 kDa, and replicase. Copyright © 2004 John Wiley & Sons, Ltd.