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The element sulfur is almost omnipresent in all natural proteomes and plays a key role in protein quantification. Incorporated in the amino acids cysteine and methionine, it has been served as target for many protein-labeling reactions in classic quantitative proteomic approaches based on electrospray or MALDI mass spectrometry. This critical review discusses the potential and limitations of sulfur isotope dilution analysis (IDA) by inductively coupled plasma-mass spectrometry (ICP-MS) for absolute protein quantification. The development of this approach was made possible due to the improved sensitivity and accuracy of sulfur isotope ratio measurement by ICP-MS in recent years. The unique feature of ICP-MS, compound-independent ionization, enables compound (species)-unspecific sulfur IDA. This has the main advantage that only one generic sulfur standard (i.e., one isotopically labeled sulfur spike) is required to quantify each peptide or protein in a sample provided that they are completely separated in chromatography or electrophoresis and that their identities are known. The principles of this approach are illustrated with selected examples from the literature. The discussion includes also related fields of P/S and metal/S ratio measurements for the determination of phosphorylation degrees of proteins and stoichiometries in metalloproteins, respectively. Emerging new areas and future trends such as protein derivatization with metal tags for improved sensitivity of protein detection in ICP-MS are discussed.
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PMID:The role of sulfur and sulfur isotope dilution analysis in quantitative protein analysis. 1798 23

Eight different analytical extraction procedures commonly used to extract mercury species from biological samples were evaluated by analyzing Tuna Fish Tissue Certified Reference Material (ERM-CE464) certified for the content of total mercury and methylmercury. Speciated isotope dilution mass spectrometry (SIDMS; US Environmental Protection Agency's method 6800) was utilized to evaluate and effectively compensate for potential errors during measurement and accurately quantify mercury species using all the extraction methods. SIDMS was used to accurately evaluate species transformations during sample pretreatment, preparation and analysis protocols. The extraction methods tested in this paper were based on alkaline extraction with KOH or tetramethylammonium hydroxide; acid leaching with HCl, HNO(3) or CH(3)COOH; extraction with L: -cysteine hydrochloride; and enzymatic digestion with protease XIV. Detection of total mercury and mercury species from all extraction methods was carried out by inductively coupled plasma mass spectrometry (ICP-MS) and high-performance liquid chromatography-ICP-MS, respectively. Microwave-assisted extraction and ultrasound-assisted extraction were found to be the most efficient alkaline digestion protocols that caused the lowest levels of transformation of mercury species (6% or less). Extraction with 5 M HCl or enzymatic digestion with protease resulted in the second-highest extraction efficiency, with relatively lower transformation of methylmercury to inorganic mercury (3 and 1.4%, respectively). Despite frequent use of acid leaching for the extraction of mercury species from tuna fish samples, the lowest extraction efficiencies and the highest mercury species transformation were obtained when microwave-assisted extraction with 4 M HNO(3) or CH(3)COOH was used. Transformations as high as 30% were found using some literature protocols; however, all the extractions tested produced accurate quantitation when corrected in accordance with the SIDMS method standardized in the US Environmental Protection Agency's method 6800. [figure: see text]
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PMID:Comparison of methods with respect to efficiencies, recoveries, and quantitation of mercury species interconversions in food demonstrated using tuna fish. 1831 38

Speciation of mercury in salmon egg cell cytoplasm was investigated by surfactant-mediated high-performance liquid chromatography/inductively coupled plasma mass spectrometry (HPLC/ICP-MS), where an ODS (octadecylsilica) column coated with a bile acid derivative, CHAPS (3-[(3-cholamidopropyl)-dimethylammonio]-1-propane sulfonate), was used for species separation. Prior to the speciation analysis, total Hg in the cell cytoplasm was determined by ICP-MS at m/z 202 in a flow injection mode. For the precise measurement, salmon egg cell cytoplasm was diluted five-fold with 0.1M Tris (Tris(hydroxymethyl)aminomethane)-HNO(3) buffer solution, and the standard addition method was employed. Thus, the total concentration of Hg in cell cytoplasm was estimated to be 12.4ngg(-1) on the wet weight basis. Next, the cell cytoplasm diluted five-fold with 0.1M Tris-HNO(3) buffer solution was analyzed by surfactant-mediated HPLC with the dual detection system of a UV absorption detector and an ICP-MS instrument. Two peaks corresponding to some proteins and small molecules were mainly observed in those chromatograms. When salmon egg cell cytoplasm was diluted five-fold with 0.01M Tris buffer solution or pure water, some precipitates appeared probably because of precipitation of hydrophobic proteins in cytoplasm. After the precipitates were eliminated with a membrane filter, the filtrate was subjected to the analysis by surfactant-mediated HPLC/UV/ICP-MS. As a result, the peaks for small molecular species of Hg were clearly observed at the retention time near 4.0min (corresponding to low-molecular weight zone) in the chromatograms with UV absorption detection as well as with Hg- and S-specific ICP-MS detections. The small molecule bound with Hg was identified as cysteine through the cysteine-spiked experiment. In addition, the protein fraction on the chromatogram obtained by using the CHAPS-coated ODS column was further analyzed by SEC (size exclusion chromatography). Consequently, several protein peaks with molecular weight of 300, 50 and 12kDa were observed in all the detections of UV absorption, Hg and Se, although two peaks among them were coincident in the case of S. These results indicate that Hg in salmon egg cell cytoplasm binds with proteins containing selenocysteine and/or cysteine residues in proteins.
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PMID:Speciation of mercury in salmon egg cell cytoplasm in relation with metallomics research. 1897 Mar 45

Solid-phase extraction (SPE) based on molecularly imprinted polymers (MIPs) were used to develop selective separation and preconcentration for methylmercury ion from complex matrixes. In this study, an ion-imprinting polymer was prepared to make artificial organomercury lyase preorganizing three methacryloyl-(L)-cysteine methylester (MAC) monomers and one methylmercury ion in a three-coordinate form by template polymerization, with the goal preparing a solid-phase which has the high selectivity for methylmercury ions. Methylmercury-imprinted beads were produced by a dispersion polymerization technique with use methylmercury-methacryloyl-(L)-cysteine (MM-MAC) complex monomer and ethylene glycoldimethacrylate (EDMA). After removal of methylmercury ions, methylmercury-imprinted beads were used for solid-phase extraction and determination of mercury compounds. Methylmercury adsorption and selectivity studies of methylmercury versus other metal ions which Hg(II), Zn(II), Pb(II) and Cd(II) were reported and distribution and selectivity coefficients of these ions with respect to methylmercury were calculated here. ICP-OES and HPLC-DAD determinations of methylmercury and mercury ions in the certified reference, LUTS-1 from the National Research Council of Canada and synthetic sea water showed that the interfering matrix had been almost removed during preconcentration. The methylmercury-imprinted solid-phase as mimic receptor was good enough for methylmercury determination in complex matrixes.
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PMID:Mimicking receptor for methylmercury preconcentration based on ion-imprinting. 1907 62

The need of analytical methods for absolute quantitative protein analysis spurred research on new developments in recent years. In this work, a novel approach was developed for accurate absolute peptide quantification based on metal labeling with lutetium diethylenetriamine pentaacetic acid (Lu-DTPA) and nanoflow high-performance liquid chromatography-inductively coupled plasma isotope dilution mass spectrometry (nanoHPLC-ICP-IDMS). In a two-step procedure peptides were derivatized at amino groups with diethylenetriamine pentaacetic anhydride (DTPAA) followed by chelation of lutetium. Electrospray ionization mass spectrometry (ESI MS) of the reaction product demonstrated highly specific peptide labeling. Under optimized nanoHPLC conditions the labeled peptides were baseline-separated, and the excess labeling reagent did not interfere. A 176Lu-labeled spike was continuously added to the column effluent for quantification by ICP-IDMS. The recovery of a Lu-DTPA-labeled standard peptide was close to 100% indicating high labeling efficiency and accurate absolute quantification. The precision of the entire method was 4.9%. The detection limit for Lu-DTPA-tagged peptides was 179 amol demonstrating that lutetium-specific peptide quantification was by 4 orders of magnitude more sensitive than detection by natural sulfur atoms present in cysteine or methionine residues. Furthermore, the application to peptides in insulin tryptic digest allowed the identification of interfering reagents decreasing the labeling efficiency. An additional advantage of this novel approach is the analysis of peptides, which do not naturally feature ICPMS-detectable elements.
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PMID:Absolute peptide quantification by lutetium labeling and nanoHPLC-ICPMS with isotope dilution analysis. 1911 64

Metallothioneins (MTs) are a family of low molecular weight, cysteine-rich and metal-binding functional proteins. Transgenic MT mushroom can be used as functional food additives, but its zinc-enriching ability has not been studied systemically until now. The zinc contents in mycelia of transgenic MT mushroom (Pleurotus ostreatus) and wild type mushroom mycelia cultivated in different zinc concentration media were analyzed by ICP-OES. The growth status, zinc-enriching ability and degree of zinc in organic form (DZOF) were also analyzed. Results showed that MT mushroom mycelia grew rapidly, but the growth was inhibited when the zinc content in solid media was higher than 1.6 mmol x L(-1). MT mushroom mycelia could enrich more zinc than that of wild type, and the zinc content in MT mushroom mycelia could be 2.56-27.49 mg x kg(-1) when it was cultivated in a liquid media with 0.6-1.2 mmol x L(-1) zinc. DZOF of MT mushroom mycelia in a liquid media with 0.6 mmol x L(-1) zinc at 7 d was significantly higher (88.7%) than that in the wild type (82.1%, alpha = 0.05), but there was no significant difference in DZOF when the MT mushroom mycelia was cultivated in a liquid media with different zinc content at 7 d.
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PMID:[Effect of cultivation in zinc media on the growth of and the degree of zinc in organic form in transgenic metallothionein mushroom]. 1945 31

It has been proposed that the natural cysteine peptidase inhibitor ICP of Leishmania mexicana protects the protozoan parasite from insect host proteolytic enzymes, thereby promoting survival. To test this hypothesis, L. mexicana mutants deficient in ICP were evaluated for their ability to develop in the sand fly Lutzomyia longipalpis. No significant differences were found between the wild-type parasites, two independently derived ICP-deficient mutants, or mutants overexpressing ICP; all lines developed similarly in the sand fly midgut and produced heavy late-stage infections. In addition, recombinant L. mexicana ICP did not inhibit peptidase activity of the midgut extracts in vitro. We conclude that ICP has no major role in promoting survival of L. mexicana in the vectorial part of its life cycle in L. longipalpis.
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PMID:Inhibitor of cysteine peptidase does not influence the development of Leishmania mexicana in Lutzomyia longipalpis. 1949 33

In this work, the quantification of two mercury species (Hg(2+) and CH(3)Hg(+)) in fish tissues has been revisited. The originality of our approach relies on the use of Bi(3+) as internal standard (IS) and on the modification of typical extraction conditions. The IS (125 microl, 1000 microg l(-1) Bi(3+)) was added to the aliquot of fresh fish tissue (400-500 mg). A high-speed blender and ultrasound-assisted homogenization/extraction was carried out in the presence of perchloric acid (1.5 ml, 0.6 mol l(-1)), l-cysteine (500 microl, 0.75 mol l(-1)) and 500 microl toluene:methanol (1:1). Perchloric acid was used for protein denaturation and precipitation, toluene helped to destroy lipid structures potentially sequestering CH(3)Hg(+), L-cysteine was used to form water-soluble complexes with Bi(3+), Hg(2+) and CH(3)Hg(+). The excess of perchloric acid was eliminated by addition of potassium hydroxide (pH 5 with acetic acid). The obtained extract, was diluted with the mobile phase (1:1) and introduced (20 microl) to the reversed phase HPLC-ICP-MS system. The separation was achieved by isocratic elution (2.5 mmol l(-1) cysteine, 12.5 mmol l(-1) (NH(4))(2)HPO(4), 0.05% triethylamine, pH 7.0:methanol (96:4)) at a flow rate 0.6 ml min(-1). Column effluent was on-line introduced to ICP-MS for specific detection of (202)Hg, (200)Hg and (209)Bi. Analytical signal was defined as the ratio between (202)Hg/(209)Bi peak areas. The detection limits evaluated for Hg(2+) and CH(3)Hg(+) were 0.8 and 0.7 microg l(-1). Recovery of the procedure, calculated as the sum of species concentrations found in the sample with respect to total ICP-MS-determined Hg was 91.9% for king mackerel muscle and 89.5% for red snapper liver. In the standard addition experiments, the recovery results were 98.9% for Hg(2+) and 100.6% for CH(3)Hg(+). It should be stressed that the use of Bi(3+) as IS enabled to improve analytical performance by compensating for incomplete extraction and for imprecision of sample handling during relatively non-rigorous protocol.
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PMID:Analytical speciation of mercury in fish tissues by reversed phase liquid chromatography-inductively coupled plasma mass spectrometry with Bi(3+) as internal standard. 1957 34

In sulfidic environments, hydride generation-based approaches are not suitable for arsenic determination because thioarsenates which can constitute the predominant arsenic species under these conditions (> 80% of total arsenic) are completely ignored. Sample acidification for preservation or during hydride generation leads to loss of total inorganic arsenic due to precipitation of arsenic-sulfur phases. Total concentrations can be determined correctly using 1% potassium iodide as prereducing agent while with L-cysteine (0.16 mol L(-1)), transformation of tetra-, tri-, and dithioarsenate to arsenite remains incomplete. By decreasing the original sample pH, hydride generation destroys thioarsenate species distribution because only monothioarsenate is stable over the whole pH range. Dithioarsenate transforms to arsenite below pH 4. Tetrathioarsenate transforms to trithioarsenate (pH 11.9) which subsequently transforms to arsenite (pH 5.6), followed by precipitation of arsenic-sulfur phases below pH 5. It is thus impossible to determine thioarsenates by hydride generation. The "As(III)"--fraction contains tetra-, tri-, and some dithioarsenate as well as arsenite, while monothioarsenate is determined with arsenate as "As(V)". Different analytical setups have substantial impact on thioarsenate hydride-generation behavior, thus provide little comparability and render reinterpretation of existing arsenic hydride-generation speciation data from sulfidic environments impossible. In natural geothermal water samples from Yellowstone National Park, total arsenic concentrations determined by ICP-MS and by HG-AFS with prereductant agreed well (< 6% relative difference). Speciation results deviated from the behavior predicted for thioarsenates from laboratory experiments, probably due to matrix effects.
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PMID:A critical investigation of hydride generation-based arsenic speciation in sulfidic waters. 1967 99

Despite the necessity to differentiate chemical species of mercury in clinical specimens, there are a limited number of methods for this purpose. Then, this paper describes a simple method for the determination of methylmercury and inorganic mercury in blood by using liquid chromatography with inductively coupled mass spectrometry (LC-ICP-MS) and a fast sample preparation procedure. Prior to analysis, blood (250microL) is accurately weighed into 15-mL conical tubes. Then, an extractant solution containing mercaptoethanol, l-cysteine and HCl was added to the samples following sonication for 15min. Quantitative mercury extraction was achieved with the proposed procedure. Separation of mercury species was accomplished in less than 5min on a C18 reverse-phase column with a mobile phase containing 0.05% (v/v) mercaptoethanol, 0.4% (m/v) l-cysteine, 0.06molL(-1) ammonium acetate and 5% (v/v) methanol. The method detection limits were found to be 0.25microgL(-1) and 0.1microgL(-1) for inorganic mercury and methylmercury, respectively. Method accuracy is traceable to Standard Reference Material (SRM) 966 Toxic Metals in Bovine Blood from the National Institute of Standards and Technology (NIST). The proposed method was also applied to the speciation of mercury in blood samples collected from fish-eating communities and from rats exposed to thimerosal. With the proposed method there is a considerable reduction of the time of sample preparation prior to speciation of Hg by LC-ICP-MS. Finally, after the application of the proposed method, we demonstrated an interesting in vivo ethylmercury conversion to inorganic mercury.
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PMID:Methylmercury and inorganic mercury determination in blood by using liquid chromatography with inductively coupled plasma mass spectrometry and a fast sample preparation procedure. 2000 68


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