Ion-pair reversed-phase liquid chromatography for determination of polar underivatized amino acids using perfluorinated carboxylic acids as ion pairing agent

Pétritis, Konstantinos; Chaimbault, Patrick; Elfakir, Claire; Dreux, M.

doi:10.1016/s0021-9673(98)01060-7

Cited by 137 publications

(87 citation statements)

References 21 publications

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“…The increase Thus, investigation of perfluorinated carboxylic acids in pH from TFA to HFBA could cause such a switch of greater chain length seemed appropriate, as earlier due to the slightly different pK values of coma reports showed their successful application for the pounds 13 and 14. The large retention time increase separation of amino acids [32].…”

Section: Resultsmentioning

confidence: 99%

“…Uden) dietary supplementation with selenium-enriched yeast decreased cancer incidence and mortality rates carboxylic acids for the separation of amino acids by almost 50%. Increase in selenium intake by has been evaluated [32][33][34]. consuming a diet with natural selenium levels is Other nonvolatile organic selenium species, which problematic due to the low abundance of selenium in may be present in natural samples, are the selenoxcommon food [2].…”

Section: Introductionmentioning

confidence: 99%

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High-performance liquid chromatography of selenium compounds utilizing perfluorinated carboxylic acid ion-pairing agents and inductively coupled plasma and electrospray ionization mass spectrometric detection

Kotrebai

Tyson

Block

et al. 2000

Journal of Chromatography A

137

107

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

High-performance liquid chromatography of selenium compounds utilizing perfluorinated carboxylic acid ion-pairing agents and inductively coupled plasma and electrospray ionization mass spectrometric detection

Kotrebai

Tyson

Block

et al. 2000

Journal of Chromatography A

137

107

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“…Different acidic ion-pairing agents are anticipated to create changes in the elution time patterns (the amount of shift and possibly the order) since for the same mobile phase concentration, the hydrophobicity and pKa of the ion-pairing reagent will determine the amount of electrostatic interactions available in the column (assuming that the pH of the mobile phase is determined by the concentration of the ion-pairing reagent in the column) [42,43]. Indeed, for aliphatic acidic ion-pairing reagents, the longer the side chain, the more the column will behave as a dynamic cation-exchanger.…”

Section: Effect Of Different Ion-pairing Agentsmentioning

confidence: 99%

Phosphopeptide elution times in reversed-phase liquid chromatography

Kim

Pétritis

Shen

et al. 2007

Journal of Chromatography A

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Elution time shifts between 33 different peptides and their corresponding phosphopeptides ranging from 4 amino acid residues to 35 amino acids in length were systematically investigated using highresolution reversed-phase liquid chromatography (RPLC)-tandem mass spectrometry (MS/MS) analysis with trifluoroacetic acid as the ion pairing agent. Observed peptide elution time shifts for a single phosphorylation ranged from −5.28 min (for pYVPML) to +0.59 min (for HRDpSGLLDSLGR). Peptides containing a phosphotyrosine residue displayed a significant decrease in elution time following phosphorylation compared to their similar-sized peptides with phosphoserine or phosphothreonine residues. While peptide phosphorylation generally led to a decrease in the observed elution time, five peptides displayed increased elution times as a result of phosphorylation. For large peptides (= 18 amino acids), the elution time shifts due to single phosphorylation were limited (ranging between −0.48 min and +0.03 min), while the elution time shifts for small peptides (< 18 amino acids) were characterized by a larger deviation (ranging between −5.28 min and +0.59 min). The predictive capability for the observed RPLC elution time change due to phosphorylation has been suggested, which will aid in assigning confident phosphopeptide identifications and their subsequent confirmation.

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“…Similar results were obtained by raising the final concentration of TFA to 0.2%. Perfluorinated carboxylic acids with longer n-alkyl chains, such as pentafluoropropionic, heptafluorobutyric, perfluoropentanoic, perfluorohexanoic and perfluoroheptanoic acid, have been employed as alternatives to TFA for the separation of polar peptides and proteins 25,26 and for natural amino acids 27 and dipeptides. 28 Table 1).…”

Section: Optimization Of Lc and Ms Conditionsmentioning

confidence: 99%

Profiling histidine‐containing dipeptides in rat tissues by liquid chromatography/electrospray ionization tandem mass spectrometry

et al. 2004

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The histidine-containing dipeptides carnosine (CAR) and structurally related anserine (ANS) and homocarnosine (HCAR), widely distributed in vertebrate organisms, have recently been proposed as endogenous quenchers for highly cytotoxic a,b-unsaturated aldehydes generated by peroxidation. A sensitive, selective, specific and rapid liquid chromatographic/electrospray ionization tandem mass spectrometric assay was developed and validated for the simultaneous determination of these peptides in biological matrices in order to establish their plasma/tissue distribution. Samples (plasma or tissue homogenates from male rats) were prepared by protein precipitation with HClO The intra-and inter-day precisions were <10% (≤17.47% at the LOQ) and the intra-and inter-assay accuracies were within ±10% for all concentrations. The mapping profile in rat tissue gave the following results: the highest concentrations of CAR and ANS were found in skeletal muscles (soleus, gastrocnemius, tibialis), followed by the heart, cerebellum and brain (ANS below the LOQ). HCAR was found only in the brain and cerebellum. No histidine-containing dipeptides were detectable in plasma, liver, kidney and lung.

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Ion-pair reversed-phase liquid chromatography for determination of polar underivatized amino acids using perfluorinated carboxylic acids as ion pairing agent

Cited by 137 publications

References 21 publications

High-performance liquid chromatography of selenium compounds utilizing perfluorinated carboxylic acid ion-pairing agents and inductively coupled plasma and electrospray ionization mass spectrometric detection

High-performance liquid chromatography of selenium compounds utilizing perfluorinated carboxylic acid ion-pairing agents and inductively coupled plasma and electrospray ionization mass spectrometric detection

Phosphopeptide elution times in reversed-phase liquid chromatography

Profiling histidine‐containing dipeptides in rat tissues by liquid chromatography/electrospray ionization tandem mass spectrometry

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