Qiuquan Wang

Online pre-reduction of selenium(VI) with a newly designed UV/TiO2 photocatalysis reduction device

The online pre-reduction of selenium(VI) has been achieved on a newly designed UV/TiO2 photocatalysis reduction device; its vapor generation efficiency has been improved up to 53.3%.

Vapour generation at a UV/TiO2 photocatalysis reaction device for determination and speciation of mercury by AFS and HPLC-AFS

In this study we report a method for direct vapor generation of mercury species on nano TiO2 under UV irradiation in the presence of a formic acid and sodium formate mixture as a hole scavenger. A novelly designed UV/TiO2 photocatalysis reaction device (UV/TiO2 PCRD) was used as an effective sample introduction unit and an interface for mercury species determination by atomic fluorescence spectrometry (AFS) and speciation by HPLC-AFS for the first time. The detection limits of 10, 20, 30 and 70 pg mL � 1 of mercury chloride, methylmercury chloride, ethylmercury chloride and phenylmercury chloride, respectively, were achieved by AFS using flow injection mode. Compared with the traditional KBH4/NaOH-HCl system, UV/TiO2 PCRD is a superior alternative for online vapor generation of Hg species.

Mechanisms of chemical generation of volatile hydrides for trace element determination (IUPAC Technical Report)

Aqueous-phase chemical generation of volatile hydrides (CHG) by derivatization with borane complexes is one of the most powerful and widely employed methods for determination and speciation analysis of trace and ultratrace elements (viz. Ge, Sn, Pb, As, Sb, Bi, Se, Te, Hg, Cd, and, more recently, several transition and noble metals) when coupled with atomic and mass spectrometric detection techniques. Analytical CHG is still dominated by erroneous concepts, which have been disseminated and consolidated within the analytical scientific community over the course of many years. The overall approach to CHG has thus remained completely empirical, which hinders possibilities for further development. This report is focused on the rationalization and clarification of fundamental aspects related to CHG: (i) mechanism of hydrolysis of borane complexes; (ii) mechanism of hydrogen transfer from the borane complex to the analytical substrate; (iii) mechanisms through which the different chemical reaction conditions control the CHG process; and (iv) mechanism of action of chemical additives and foreign species. Enhanced comprehension of these different mechanisms and their mutual influence can be achieved in light of the present state of knowledge. This provides the tools to explain the reactivity of a CHG system and contributes to the clarification of several controversial aspects and the elimination of erroneous concepts in CHG.

Absolute Quantification of Intact Proteins via 1,4,7,10-Tetraazacyclododecane-1,4,7-trisacetic acid-10-Maleimidoethylacetamide-Europium Labeling and HPLC Coupled with Species-Unspecific Isotope Dilution ICPMS

Quantitative proteomics requires novel analytical methodology to fill the gap related to absolute protein abundance in different physiological conditions. In this paper, we demonstrate a proof-of-concept study for absolute protein quantification. 1,4,7,10-Tetraazacyclododecane-1,4,7-trisacetic acid-10-maleimidoethylacetamide (MMA-DOTA) loaded with Eu was used to label lysozyme, insulin, and ribonuclease A, and they were subsequently quantified using HPLC coupled with (153)Eu species-unspecific isotope dilution inductively coupled plasma mass spectrometry (ICPMS). Labeling procedures were optimized using electrospray ionization mass spectrometry (ESI-MS) based on the labeling efficiency and specificity of the three intact proteins, which suggested that 10-fold or higher MMA-DOTA to cysteine sulphydryl rates at pH from 6.8 to 7.6 and 47 degrees C for 40 min were optimal conditions for the conjugation of the reduced-form proteins and that a 5-fold excess of Eu with respect to the DOTA present in the MMA-DOTA-conjugated proteins and pH 5.8 are optimal for Eu labeling. Subsequently, these three MMA-DOTA-Eu-labeled proteins were digested with trypsin, and the tryptic peptides were quantified via HPLC coupled with (153)Eu species-unspecific isotope dilution ICPMS. The results for the protein studied indicated that not only could 100% digestion efficiency not be achieved but also the resulting peptides needed a chromatographic separation at higher resolution. On the other hand, the labeled intact proteins were quantified without tryptic digestion. The average recovery was found to be 97.9% in six independent experiments, and the precision was evaluated to be 5.8% at the 10 pmol L(-1) level. The detection limits (3sigma) were determined to be 0.819, 1.638, and 0.819 fmol for lysozyme, the A chain of insulin, and ribonuclease A, respectively, using ICPMS with a normal concentric pneumatic nebulizer. These results demonstrated that high-quality absolute protein quantification could be achieved through labeling the intact proteins but not the tryptic peptides, implying that intact proteins may be more feasible and practical targets than tryptic peptides for ICPMS-based absolute protein quantification.

Different alkyl dimethacrylate mediated stearyl methacrylate monoliths for improving separation efficiency of typical alkylbenzenes and proteins

Monoliths were prepared in 530 microm I.D. fused silica capillaries via in situ copolymerization of stearyl methacrylate (SMA) with a dimethacrylate cross-linker in the presence of a binary porogenic solvent containing tert.-butanol and 1,4-butanediol. Alkyl dimethacrylate cross-linkers other than the monomer were used to tune the monolith properties, and, as a result, an increase in the hydrophobicity of the final monoliths (the methylene selectivity [Formula: see text] increased from 1.396 to 1.475) was observed through an increase in the molecular chain length between two methacrylate units from the 0.360 nm of ethylene glycol dimethacrylate to the 1.241 nm of 1.9-nonanediol dimethacrylate. Moreover, the hydrophobicity of the final monoliths was also greatly affected by the methyl group branch in the cross-linkers, among which the 2-methyl-1,8-octanediol dimethacrylate (2-Me-1,8-ODDMA) mediated monolith exhibited the highest hydrophobicity ( [Formula: see text] was 1.482) and fastest mass transfer kinetics (C-term was 9.14 ms). Besides the effective separation of six model proteins, the poly(SMA-co-2-Me-1,8-ODDMA) monolith also showed an improved performance in the separation of alkylbenzenes. The theoretical plate numbers reached 83000plates/m and 52000 plates/m for thiourea (nonretained compound) and butylbenzene (retained compound), respectively, when using acetonitrile-water (70:30, v/v) as the mobile phase at a typical linear velocity of 1mm/s. This improved performance towards small molecules was attributed to an increased mesopore proportion in the monolith and the faster dynamic process of mass transfer arising from novel tailoring of the monolith by choosing a suitable monomer/cross-linker pair.

Lanthanide-Coded Protease-Specific Peptide-Nanoparticle Probes for a Label-Free Multiplex Protease Assay Using Element Mass Spectrometry: A Proof-of-Concept Study

National Natural Science Foundation of China[21035006, 20775062]; Basic Research 973 Project[2009CB421605]

On-line preconcentration with a novel alkyl phosphinic acid extraction resin coupled with inductively coupled plasma mass spectrometry for determination of trace rare earth elements in seawater

A newly synthesized alkyl phosphinic acid resin (APAR) was used for on-line preconcentration of trace rare earth elements (REES, lanthanides including yttrium) and then determined by inductively coupled plasma mass spectrometry. REEs in seawater could be on-line concentrated on the APAR packed column (4.6mm i.d.x50mm in length), and eluted from the column with 0.5mL 0.1molL(-1) nitric acid within 30s. An enrichment factor of nearly 400 was achieved for all REEs when the seawater sample volume was 200mL, while the matrix and coexisting spectrally interfering ions such as barium, tin and antimony could be simultaneously separated. The detection limits of this proposed method for REEs were in the range from 1.43pgL(-1) of holmium to 12.7pgL(-1) of lanthanum. The recoveries of REEs were higher than 97.9%, and the precision of the relative standard deviation (R.S.D., n=6) was less than 5%. The method has been applied to the determination of soluble REEs in seawater.

Dynamic Labeling Strategy with 204Hg-Isotopic Methylmercurithiosalicylate for Absolute Peptide and Protein Quantification

The methylmercury ion (CH(3)Hg(+)) demonstrated a high efficiency for directly labeling peptide/protein based on its specific and strong interaction with the sulfhydryl(s) in the peptide/protein and because of its smallest size among monofunctional organic mercurials studied, including methylmercury, ethylmercury, 4-(hydroxymercuric)benzoic acid, and 2,7-dibromo-4-hydroxymercurifluoresceine disodium. A simple 1:1 stoichiometry between CH(3)Hg(+) and sulfhydryl, confirmed with electrospray ionization-mass spectrometry (ESI-MS) and matrix-assisted laser desorption ionization-time-of-flight-mass spectrometry (MALDI-TOF-MS) studies, made it easy to calibrate the stoichiometry of Hg in the peptide/protein. In order to avoid the direct use of the harmful CH(3)Hg(+), in this study a CH(3)Hg(+)-equivalent tag, methylmercurithiosalicylate (CH(3)Hg-THI), and its (204)Hg-enriched homologue (CH(3)(204)Hg-THI) were synthesized, and then CH(3)Hg(+) and/or CH(3)(204)Hg(+) released from CH(3)Hg-THI and/or CH(3)(204)Hg-THI in solution were utilized to demonstrate the dynamic labeling of glutathione (GSH) and two model proteins, beta-lactoglobulin (BLG) and ovalbumin (OVA), for the first time. Furthermore, the CH(3)(204)Hg-THI isotopical labeled GSH, BLG, and OVA standards (CH(3)(204)Hg-GSH, CH(3)(204)Hg-BLG, and CH(3)(204)Hg-OVA) were used to demonstrate the feasibility of absolute peptide/protein quantification using label-specific isotope dilution inductively coupled plasma mass spectrometry (ICPMS). On the basis of the accurate and sensitive determination of Hg using ICPMS, the detection limits of GSH, BLG, and OVA could reach 45.4, 45.4, and 15.1 pmol L(-1), respectively, suggesting the possibility for low-abundance peptide/protein quantification alongside the surefire quantification of moderate and highly abundant peptide/protein.

Europium-Labeled Activity-Based Probe through Click Chemistry: Absolute Serine Protease Quantification Using 153Eu Isotope Dilution ICP/MS

Click and analyze: the titled probe was synthesized by conjugating a sulfonyl fluoride and azido unit using click chemistry to give SF-Eu, which can react specifically with serine (Ser) in the active site of serine protease (SP). Combination of the method with (153)Eu-isotope dilution ICP/MS enables absolute protein quantification of active SPs in biological samples using only one (153)Eu(NO(3))(3) isotopic standard.

Preparation and evaluation of stable coating for capillary electrophoresis using coupled chitosan as coated modifier

A coated capillary modified with a coupled chitosan (COCH) was developed by using a simple and fast (60 min) process that could be easily automated in capillary electrophoresis instrument. The COCH coating was achieved by first attaching chitosan to the capillary inner wall, and then coupling with glutaraldehyde, and rinsing chitosan again to react with glutaraldehyde. The COCH coating was stable and showed amphoteric character over the pH range of 1.8-12.0. When the pH value was lower than 4.5, the capillary surface possessed positive charges, which caused a reversal in the direction of the electroosmotic flow (EOF). The normal EOF direction could be obtained when the pH value was higher than 4.5. The COCH coating showed strong stability against 0.1 mol/L HCl, 0.1 mol/L NaOH and other solvents compared with conventional chitosan coating. The relative standard deviation of the run-to-run, day-to-day and capillary-to-capillary coating was all below 2% for the determination of EOF. The COCH-modified capillary was applied to acidic and basic proteins analyses and high efficiency could be attained. The comparison between unmodified capillary, chitosan-modified and COCH-modified capillary for the separation of real sample, extract from Elaphglossum yoshinagae with water, was also studied. Better results could be obtained on COCH-modified capillary than the other two capillaries.