Two-Dimensional Liquid Chromatography Study of the Human Whole Saliva Proteome

The human whole saliva proteome was investigated using two-dimensional liquid chromatography (2-DLC). The 2-DLC study was able to identify, with high confidence, 102 proteins including most known salivary proteins (35), and a large number of common serum proteins (67). Peptides from proline-rich pro...

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Bibliographic Details
Published in:Journal of proteome research 2004-09, Vol.3 (5), p.1017-1023
Main Authors: Wilmarth, Phillip A, Riviere, Michael A, Rustvold, D. Leif, Lauten, Jeffrey D, Madden, Theresa E, David, Larry L
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Blood Proteins - analysis
Chromatography, Liquid
Databases, Protein
Humans
Mass Spectrometry
Molecular Sequence Data
Peptide Fragments - analysis
Peptides - analysis
Peptides - genetics
Peptides - metabolism
Proline-Rich Protein Domains
Proteome - analysis
Proteome - genetics
Saliva - chemistry
Saliva - metabolism
Salivary Proteins and Peptides - analysis
Salivary Proteins and Peptides - genetics
Salivary Proteins and Peptides - metabolism
Trypsin - metabolism
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Summary:The human whole saliva proteome was investigated using two-dimensional liquid chromatography (2-DLC). The 2-DLC study was able to identify, with high confidence, 102 proteins including most known salivary proteins (35), and a large number of common serum proteins (67). Peptides from proline-rich proteins, abundant in saliva, had unusual cleavage sites and were frequently only partially tryptic. Three proteins not previously observed in human saliva were also detected. Significantly greater numbers of identified proteins, including high molecular weight, low molecular weight, and proline-rich proteins, were found with 2-DLC compared to previously reported two-dimensional gel electrophoresis studies. Keywords: human saliva • two-dimensional liquid chromatography • mass spectrometry
ISSN:1535-3893
1535-3907
DOI:10.1021/pr049911o