The separation of dimethylarsinic acid, methylarsonous acid, methylarsonic acid, arsenate and dimethylarsinous acid on the Hamilton PRP-X100 anion-exchange column

Gailer, Jürgen; Madden, Sean; Cullen, William R.; Denton, M. Bonner

doi:10.1002/(sici)1099-0739(199911)13:11<837::aid-aoc924>3.0.co;2-z

Cited by 30 publications

(20 citation statements)

References 26 publications

(34 reference statements)

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“…Greater concentrations of one or more compounds led to peak overlapping. This confirms the results published by Gailer and co-workers, 10,11 who studied the separation of anionic arsenic species on the PRP X100 column in dependence of pH and phosphate concentration of the eluent. The main difference between carbonate and phosphate buffer was reversal of the elution order of DMA red and As(V).…”

Section: Resultssupporting

confidence: 91%

“…Storage of the extract resulted in an increased chromatographic recovery (Table 3) ( Table 5). The ability of CuCl/HCl to destroy arsenic-protein complexes 11 was also tested. The wool extract was mixed with 0.2 M CuCl/0.2 M HCl solution at a ratio of 1 : 10 and heated for 5 h at 37 • C. This improved the total recovery of arsenic by about 20% (Table 3).…”

Section: Arsenic Species In Water Extracts Of Woolmentioning

confidence: 99%

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Identification of arsenic species in sheep‐wool extracts by different chromatographic methods

Raab¹,

Genney²,

Meharg³

et al. 2003

Applied Organom Chemis

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Sheep on the island of North Ronaldsay (Orkney, UK) feed mostly on seaweed, which contains high concentrations of dimethylated arsenoribosides. Wool of these sheep contains dimethylated, monomethylated and inorganic arsenic, in addition to unidentified arsenic species in unbound and complexed form. Chromatographic techniques using different separation mechanisms and detectors enabled us to identify five arsenic species in water extracts of wool. The wool contained 5.2 ± 2.3 µg arsenic per gram wool. About 80% of the arsenic in wool was extracted by boiling the wool with water. The main species is dimethylarsenic, which accounted for about 75 to 85%, monomethylated arsenic at about 5% and the rest is inorganic arsenic. Depending on the separation method and condition, the chromatographic recovery of arsenic species was between 45% for the anion exchange column, 68% for the size exclusion chromatography (SEC) and 82% for the cation exchange column. The SEC revealed the occurrence of two unknown arsenic compounds, of which one was probably a high molecular mass species. Since chromatographic recovery can be improved by either treating the extract with CuCl/HCl (CAT: 90%) or longer storage of the sample (CAT: 105%), in particular for methylated arsenic species, it can be assumed that labile arsenic-protein-like coordination species occur in the extract, which cannot be speciated with conventional chromatographic methods. It is clear from our study of sheep wool that there can be different kinds of 'hidden' arsenic in biological matrices, depending on the extraction, separation and detection methods used. Hidden species can be defined as species that are not recordable by the detection system, not extractable or do not elute from chromatographic columns.

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Section: Resultssupporting

confidence: 91%

Section: Arsenic Species In Water Extracts Of Woolmentioning

confidence: 99%

Identification of arsenic species in sheep‐wool extracts by different chromatographic methods

Raab¹,

Genney²,

Meharg³

et al. 2003

Applied Organom Chemis

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“…8 In addition, investigations of the pH-dependent retention behaviour on reversed-phase and anion-exchange HPLC columns can provide very useful information about the protonation/deprotonation behaviour of arsenic compounds whose solution chemistry is not well understood. 9,10 Similarly, an appropriately chosen chromatographic technique should provide proof of the additional negative charge on [(GS) 2 AsSe] À as compared with GSSG. The additional proof of two GSH molecules being attached to the arsenicselenium moiety of [(GS) 2 AsSe] À would require a chromatographic separation of [(GS) 2 AsSe] À from the by-product, GSSG (Eqn [1]).…”

Section: Introductionmentioning

confidence: 99%

Simultaneous multielement-specific detection of a novel glutathione-arsenic-selenium ion [(GS)2AsSe]? by ICP AES after micellar size- exclusion chromatography

Gailer

Madden

Burke

et al. 2000

Appl. Organometal. Chem.

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In order to confirm the solution structure of [(GS) 2 AsSe] À (GS = glutathione), we have investigated the retention behaviour of a [(GS) 2 AsSe] À /oxidized glutathione (GSSG) mixture on a Sephadex G-25 (SF) column with Tris buffers (0.1 mol dm À3 , pH 8.0) containing various surfactants at concentrations above the critical micellar concentration (CMC): hexadecyltrimethlammonium bromide (HDTAB; 30, 40 and 50 mmol dm À3 ); dodecyltrimethylammonium bromide (DDTAB; 50 mmol dm À3 ); and sodium lauryl sulfate (SLS; 50 mmol dm À3 ). An inductively coupled plasma atomic emission spectrometer (ICP AES) provided simultaneous on-line detection of arsenic, selenium and sulfur in the column effluent. The chromatographic retention behaviour was used to investigate the association of both compounds with the positively charged micelles (HDTAB and DDTAB mobile phases). The relative strength of association with the micelles provided insight into the effective negative charge on [(GS) 2 AsSe] À and GSSG. The chromatograms obtained with 50 mmol dm À3 HDTAB indicated that two glutathione molecules are associated with the elution of an arsenic-selenium compound. Combined, these chromatographic data strongly support the spectroscopically derived solution structure of [(GS) 2 AsSe] À .

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“…The reaction mixtures were incubated at 37 °C for 2 h, and then terminated by adding H 2 O 2 to a final concentration of 3% to release the arsenicals from proteins and to oxidize all arsenic metabolites to pentavalency [16], [30]. 20 µl aliquots of the samples were separated on an anion-exchange column (PRP X-100 250 mm×4.6 mm i.d., 5 µm, Hamilton) by HPLC and analyzed by ICP-MS (Elan 9000, PerkinElmer) with the flow rate of 1.0 ml/min at room temperature [31]-[33]. The arsenical compounds were eluted with the mobile phase of 12 mM (NH 4 ) 2 HPO 4 , the pH of which was adjusted to 6.0 with H 3 PO 4 .…”

Section: Methodsmentioning

confidence: 99%

Residues in Human Arsenic (+3 Oxidation State) Methyltransferase Forming Potential Hydrogen Bond Network around S-adenosylmethionine

Cao

Wang

et al. 2013

PLoS ONE

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Residues Tyr59, Gly78, Ser79, Met103, Gln107, Ile136 and Glu137 in human arsenic (+3 oxidation state) methyltransferase (hAS3MT) were deduced to form a potential hydrogen bond network around S-adenosylmethionine (SAM) from the sequence alignment between Cyanidioschyzon merolae arsenite S-adenosylmethyltransferase (CmArsM) and hAS3MT. Herein, seven mutants Y59A, G78A, S79A, M103A, Q107A, I136A and E137A were obtained. Their catalytic activities and conformations were characterized and models were built. Y59A and G78A were completely inactive. Only 7.0%, 10.6% and 13.8% inorganic arsenic (iAs) was transformed to monomethylated arsenicals (MMA) when M103A, Q107A and I136A were used as the enzyme. The Vmax (the maximal velocity of the reaction) values of M103A, Q107A, I136A and E137A were decreased to 8%, 22%, 15% and 50% of that of WT-hAS3MT, respectively. The KM(SAM) (the Michaelis constant for SAM) values of mutants M103A, I136A and E137A were 15.7, 8.9 and 5.1 fold higher than that of WT-hAS3MT, respectively, indicating that their affinities for SAM were weakened. The altered microenvironment of SAM and the reduced capacity of binding arsenic deduced from KM(As) (the Michaelis constant for iAs) value probably synergetically reduced the catalytic activity of Q107A. The catalytic activity of S79A was higher than that of WT despite of the higher KM(SAM), suggesting that Ser79 did not impact the catalytic activity of hAS3MT. In short, residues Tyr59 and Gly78 significantly influenced the catalytic activity of hAS3MT as well as Met103, Ile136 and Glu137 because they were closely associated with SAM-binding, while residue Gln107 did not affect SAM-binding regardless of affecting the catalytic activity of hAS3MT. Modeling and our experimental results suggest that the adenine ring of SAM is sandwiched between Ile136 and Met103, the amide group of SAM is hydrogen bonded to Gly78 in hAS3MT and SAM is bonded to Tyr59 with van der Waals, cation-π and hydrogen bonding contacts.

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The separation of dimethylarsinic acid, methylarsonous acid, methylarsonic acid, arsenate and dimethylarsinous acid on the Hamilton PRP-X100 anion-exchange column

Cited by 30 publications

References 26 publications

Identification of arsenic species in sheep‐wool extracts by different chromatographic methods

Identification of arsenic species in sheep‐wool extracts by different chromatographic methods

Simultaneous multielement-specific detection of a novel glutathione-arsenic-selenium ion [(GS)2AsSe]? by ICP AES after micellar size- exclusion chromatography

Residues in Human Arsenic (+3 Oxidation State) Methyltransferase Forming Potential Hydrogen Bond Network around S-adenosylmethionine

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