Search PubMed⌕ Search
Home/Archive/PubMed

PubMed · 10941681

Ion-pair solid-phase extraction.

M C Carson
View original source ↗Export metadata ↓

Abstract

Solid-phase extraction (SPE) is a technique widely employed by analytical chemists. SPE cartridges are available in a wide variety of formats containing media with diverse chemistries. This paper will review ion-pair SPE, one of the less frequently applied, and presumably less well-known techniques. Advantages of this technique over more conventional reversed-phase or ion-exchange SPE include selectivity, compatibility with rapid evaporative concentration, and potential application to multiclass multiresidue analysis.

Explore related subjects

Chromatography, Ion ExchangeJournal ArticleReview

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

M C Carson. 2000-07-14. Ion-pair solid-phase extraction.. https://doi.org/10.1016/s0021-9673(00)00471-4

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2001

Speciation of selenium in plant water extracts by ion exchange chromatography-hydride generation atomic absorption spectrometry.

Determination of selenium (Se) speciation in plants is important in studying the bioavailability and toxicity of Se in Se-contaminated soil/sediment. In this study, we used an anion exchange resin (Dowex 1-10X) to separate Se into non-amino acid organic Se, Se-amino acids, selenite (Se [IV]) and selenate (Se [VI]) in a plant (Stanleya pinnata) extract. The hydride generation atomic absorption spectrometry (HGAAS) was used to determine concentrations of these Se compounds in plant extracts. Results showed that Se compounds can be quantitatively separated by the resin column. Recovery of five spiked standard Se compounds (trimethylselenonium ion (TMSe+), dimethylselenoxide (DMSeO), selenomethionine (Semet), Se [IV] and Se [VII]) in the plant extract ranged from 92.9 to 103%. Water extractable Se accounted for 60.4-72.6% of the total Se in the plant. Among the soluble Se compounds in the plant extract, Se-amino acids were 73-85.5%, Se [VI] ranged from 7.5 to 19.5% and non-amino acid organic Se was less than 7%. Se [IV] in most samples was below the detection limit (1 microg/g). This study showed that considerable amounts of the accumulated Se [VI] in the plant was metabolized to Se-amino acids during growth of the plant.

Chromatography, Ion Exchange↗
PubMed2001

Development of a new method for the quantitative analysis of the extracellular polysaccharide of Neisseria meningitidis serogroup A by use of high-performance anion-exchange chromatography with pulsed-amperometric detection.

A new method for the quantitative determination of Neisseria meningitidis group A (MenA) capsular polysaccharide (CPS) has been developed. The method is based on trifluoracetic acid (TFA) hydrolysis of the CPS (2 M at 80 degrees C for 3 h), followed by chromatographic separation and quantification of the liberated mannosamine-6-phosphate from the area of the peak obtained using an IonPac AS11 column coupled to the sensitive pulsed amperometric detector ED40. The highly selective nature of this method circumvents the interference problems associated with the classical method based on a colorimetric assay for phosphorus. Provided that suitable hydrolysis conditions can be found, this chromatographic approach might be applicable to the quantification of other bacterial antigens containing phosphorylated sugars such as meningococcal groups H, L, X and Z, and pneumococcal serotypes 6, 10A and 19.

Chromatography, Ion Exchange↗
PubMed2001

The H2 sensor of Ralstonia eutropha. Biochemical characteristics, spectroscopic properties, and its interaction with a histidine protein kinase.

Previous genetic studies have revealed a multicomponent signal transduction chain, consisting of an H(2) sensor, a histidine protein kinase, and a response regulator, which controls hydrogenase gene transcription in the proteobacterium Ralstonia eutropha. In this study, we isolated the H(2) sensor and demonstrated that the purified protein forms a complex with the histidine protein kinase. Biochemical and spectroscopic analysis revealed that the H(2) sensor is a cytoplasmic [NiFe]-hydrogenase with unique features. The H(2)-oxidizing activity was 2 orders of magnitude lower than that of standard hydrogenases and insensitive to oxygen, carbon monoxide, and acetylene. Interestingly, only H(2) production but no HD formation was detected in the D(2)/H(+) exchange assay. Fourier transform infrared data showed an active site similar to that of standard [NiFe]-hydrogenases. It is suggested that the protein environment accounts for a restricted gas diffusion and for the typical kinetic parameters of the H(2) sensor. EPR analysis demonstrated that the [4Fe-4S] clusters within the small subunit were not reduced under hydrogen even in the presence of dithionite. Optical spectra revealed the presence of a novel, redox-active, n = 2 chromophore that is reduced by H(2). The possible involvement of this chromophore in signal transduction is discussed.

Chromatography, Ion Exchange↗