Salivary protein/peptide profiling with SELDI-TOF-MS

R.G. Schipper; A. Loof; J. de Groot; L.F. Harthoorn; W. van Heerde; E. Dransfield

doi:10.1196/annals.1384.010

Salivary protein/peptide profiling with SELDI-TOF-MS

R.G. Schipper, A. Loof, J. de Groot, L.F. Harthoorn, W. van Heerde, E. Dransfield

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

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Abstract

In this study, large-scale profiling of salivary proteins and peptides ranging from 2 to 100 kDa was demonstrated using surface-enhanced laser desorption/ionization¿time of flight¿mass spectrometry (SELDI-TOF-MS). Results show that chip surface type and sample type critically affect the amount and composition of detected salivary proteins. Delayed processing time resulted in both increase and decrease of peak numbers consistent with proteolysis. SELDI-TOF-MS profiles also changed, depending on storage temperature, although sample processing by centrifugation and numbers of freeze¿thaw cycles had a minimal impact. In conclusion, SELDI-TOF-MS offers a simple, rapid, high-throughput technique for profiling low-mass (

Original language	English
Pages (from-to)	498-503
Journal	Annals of the New York Academy Of Sciences
Volume	1098
DOIs	https://doi.org/10.1196/annals.1384.010
Publication status	Published - 2007

Keywords

human whole saliva
2-dimensional gel-electrophoresis
molecular-weight peptides
flight mass-spectrometry
liquid-chromatography
protein-components
proteomic analysis
identification
histatins

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10.1196/annals.1384.010

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title = "Salivary protein/peptide profiling with SELDI-TOF-MS",

abstract = "In this study, large-scale profiling of salivary proteins and peptides ranging from 2 to 100 kDa was demonstrated using surface-enhanced laser desorption/ionization¿time of flight¿mass spectrometry (SELDI-TOF-MS). Results show that chip surface type and sample type critically affect the amount and composition of detected salivary proteins. Delayed processing time resulted in both increase and decrease of peak numbers consistent with proteolysis. SELDI-TOF-MS profiles also changed, depending on storage temperature, although sample processing by centrifugation and numbers of freeze¿thaw cycles had a minimal impact. In conclusion, SELDI-TOF-MS offers a simple, rapid, high-throughput technique for profiling low-mass (",

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author = "R.G. Schipper and A. Loof and {de Groot}, J. and L.F. Harthoorn and {van Heerde}, W. and E. Dransfield",

year = "2007",

doi = "10.1196/annals.1384.010",

language = "English",

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pages = "498--503",

journal = "Annals of the New York Academy Of Sciences",

issn = "0077-8923",

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T1 - Salivary protein/peptide profiling with SELDI-TOF-MS

AU - Schipper, R.G.

AU - Loof, A.

AU - de Groot, J.

AU - Harthoorn, L.F.

AU - van Heerde, W.

AU - Dransfield, E.

PY - 2007

Y1 - 2007

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AB - In this study, large-scale profiling of salivary proteins and peptides ranging from 2 to 100 kDa was demonstrated using surface-enhanced laser desorption/ionization¿time of flight¿mass spectrometry (SELDI-TOF-MS). Results show that chip surface type and sample type critically affect the amount and composition of detected salivary proteins. Delayed processing time resulted in both increase and decrease of peak numbers consistent with proteolysis. SELDI-TOF-MS profiles also changed, depending on storage temperature, although sample processing by centrifugation and numbers of freeze¿thaw cycles had a minimal impact. In conclusion, SELDI-TOF-MS offers a simple, rapid, high-throughput technique for profiling low-mass (

KW - human whole saliva

KW - 2-dimensional gel-electrophoresis

KW - molecular-weight peptides

KW - flight mass-spectrometry

KW - liquid-chromatography

KW - protein-components

KW - proteomic analysis

KW - identification

KW - histatins

U2 - 10.1196/annals.1384.010

DO - 10.1196/annals.1384.010

M3 - Article

SN - 0077-8923

VL - 1098

SP - 498

EP - 503

JO - Annals of the New York Academy Of Sciences

JF - Annals of the New York Academy Of Sciences

ER -

Salivary protein/peptide profiling with SELDI-TOF-MS

Abstract

Keywords

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