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; Larry L. David

doi:10.1021/pr049911o

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, Larry L. David

Chemical Physiology and Biochemistry

Research output: Contribution to journal › Article › peer-review

124 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	1017-1023
Number of pages	7
Journal	Journal of Proteome Research
Volume	3
Issue number	5
DOIs	https://doi.org/10.1021/pr049911o
State	Published - Sep 2004

Keywords

Human saliva
Mass spectrometry
Two-dimensional liquid chromatography

ASJC Scopus subject areas

Biochemistry
Chemistry(all)

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10.1021/pr049911o

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abstract = "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, Mass spectrometry, Two-dimensional liquid chromatography",

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AU - Riviere, Michael A.

AU - Rustvold, D. Leif

AU - Lauten, Jeffrey D.

AU - Madden, Theresa E.

AU - David, Larry L.

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AB - 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.

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KW - Mass spectrometry

KW - Two-dimensional liquid chromatography

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Two-dimensional liquid chromatography study of the human whole saliva proteome

Abstract

Keywords

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