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

Phillip A. Wilmarth,*† Michael A. Riviere,† D. Leif Rustvold,† Jeffrey D. Lauten,‡ Theresa E. Madden,‡ and Larry L. David†
Departments of Integrative Biosciences and Periodontology, School of Dentistry, Oregon Health and Science University, 611 S.W. Campus Drive, Portland, Oregon 97239
Journal of Proteome Research, 2004, 3 (5), pp 1017–1023
DOI: 10.1021/pr049911o
Publication Date (Web): September 11, 2004
Copyright © 2004 American Chemical Society
*

 To whom correspondence should be addressed. E-mail:  wilmarth@ohsu.edu.

,
†

 Department of Integrative Biosciences.

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‡

 Department of Periodontology.

Abstract

Abstract Image

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

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History

  • Published In Issue October 11, 2004
  • Received May 7, 2004

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