Abstract
A novel generic approach based on precolumn isotope dilution nanoHPLC-ICPMS analysis was developed for the accurate absolute quantification of sulfur-containing peptides. A 34S-labeled, species-unspecific sulfur spike (sulfate), noninteracting with analyte peptides under the optimized HPLC condition, was added directly to the chromatographic eluents. Thus a generic sulfur standard permanently present during analysis was used for peptide quantification. Interference-free detection of the 32S and 34S isotopes in ICPMS was achieved by eliminating O2 + ions in a collision cell using Xe gas at 130 μL min -1. The detection limit for sulfur was 45 μg L-1 which corresponded to 1-2 pmol of individual peptides. The method was validated by the analysis of a standard peptide solution showing high accuracy (recovery 103%) and good precision (RSD 2.1%). The combination of nanoHPLC-ICP IDMS with nanoHPLC-ESI MS/MS allowed the precise quantification and identification of sulfur-containing peptides in tryptic digests of human serum albumin and salt-induced yeast protein (SIP 18) at the picomole level.
| Original language | English |
|---|---|
| Pages (from-to) | 2859-2868 |
| Number of pages | 10 |
| Journal | Analytical Chemistry |
| Volume | 79 |
| Issue number | 7 |
| DOIs | |
| Publication status | Published - 1 Apr 2007 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Analytical Chemistry
Cite this
Precolumn isotope dilution analysis in nanoHPLC-ICPMS for absolute quantification of sulfur-containing peptides. / Schaumlöffel, Dirk; Giusti, Pierre; Preud'Homme, Hugues; Szpunar, Joanna; Łobiński, Ryszard.
In: Analytical Chemistry, Vol. 79, No. 7, 01.04.2007, p. 2859-2868.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Precolumn isotope dilution analysis in nanoHPLC-ICPMS for absolute quantification of sulfur-containing peptides
AU - Schaumlöffel, Dirk
AU - Giusti, Pierre
AU - Preud'Homme, Hugues
AU - Szpunar, Joanna
AU - Łobiński, Ryszard
PY - 2007/4/1
Y1 - 2007/4/1
N2 - A novel generic approach based on precolumn isotope dilution nanoHPLC-ICPMS analysis was developed for the accurate absolute quantification of sulfur-containing peptides. A 34S-labeled, species-unspecific sulfur spike (sulfate), noninteracting with analyte peptides under the optimized HPLC condition, was added directly to the chromatographic eluents. Thus a generic sulfur standard permanently present during analysis was used for peptide quantification. Interference-free detection of the 32S and 34S isotopes in ICPMS was achieved by eliminating O2 + ions in a collision cell using Xe gas at 130 μL min -1. The detection limit for sulfur was 45 μg L-1 which corresponded to 1-2 pmol of individual peptides. The method was validated by the analysis of a standard peptide solution showing high accuracy (recovery 103%) and good precision (RSD 2.1%). The combination of nanoHPLC-ICP IDMS with nanoHPLC-ESI MS/MS allowed the precise quantification and identification of sulfur-containing peptides in tryptic digests of human serum albumin and salt-induced yeast protein (SIP 18) at the picomole level.
AB - A novel generic approach based on precolumn isotope dilution nanoHPLC-ICPMS analysis was developed for the accurate absolute quantification of sulfur-containing peptides. A 34S-labeled, species-unspecific sulfur spike (sulfate), noninteracting with analyte peptides under the optimized HPLC condition, was added directly to the chromatographic eluents. Thus a generic sulfur standard permanently present during analysis was used for peptide quantification. Interference-free detection of the 32S and 34S isotopes in ICPMS was achieved by eliminating O2 + ions in a collision cell using Xe gas at 130 μL min -1. The detection limit for sulfur was 45 μg L-1 which corresponded to 1-2 pmol of individual peptides. The method was validated by the analysis of a standard peptide solution showing high accuracy (recovery 103%) and good precision (RSD 2.1%). The combination of nanoHPLC-ICP IDMS with nanoHPLC-ESI MS/MS allowed the precise quantification and identification of sulfur-containing peptides in tryptic digests of human serum albumin and salt-induced yeast protein (SIP 18) at the picomole level.
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UR - http://www.scopus.com/inward/citedby.url?scp=34247130048&partnerID=8YFLogxK
U2 - 10.1021/ac061864r
DO - 10.1021/ac061864r
M3 - Article
C2 - 17309230
AN - SCOPUS:34247130048
VL - 79
SP - 2859
EP - 2868
JO - Analytical Chemistry
JF - Analytical Chemistry
SN - 0003-2700
IS - 7
ER -