A mixed spike containing 119Sn-enriched monobutyltin (MBT), dibutyltin (DBT), and tributyltin (TBT) was prepared by direct butylation of 119Sn-enriched tin metal using a 1:3 molar excess of butyl chloride with iodide and triethylamine as catalysts. The isotopic composition of the different tin species in the spike solution was determined by gas chromatography- ICPMS after aqueous ethylation using sodium tetraethylborate. Reverse isotope dilution analysis was used for the characterization of the spike by means of natural MBT, DBT, and TBT standards. No species transformation was evident during derivatization from the reverse isotope dilution experiments based on the measured isotope ratios both before and after spiking. The mixed spike was applied to the simultaneous analysis of MBT, DBT, and TBT in certified reference materials, PACS-2 and CRM 646, with satisfactory results.
Water-soluble luminescent CdSe quantum dots surface-modified with 2-mercaptoethane sulfonate were synthesized for the selective determination of free cyanide in aqueous solution with high sensitivity (detection limit of 1.1 x 10(-6) M), via analyte-induced changes in their photoluminescence after photoactivation.
The interactions of various insulin mimetic oxovanadium(IV) compounds with serum proteins were studied in model systems and in ex vivo samples. For the modeling study, an earlier in situ method was extended and applied to the formation of ternary complexes of apotransferrin (apoTf)-V(IV)O-maltol (mal) and 1,2-dimethyl-3-hydroxy-4(1H)-pyridinone (dhp). Both systems were evaluated via simultaneous CD and EPR measurements. Determination of the formation constants of the ternary complexes allowed the calculation of more accurate stability constants for the V(IV)O-apoTf parent complexes and establishment of a better model for drug speciation in serum. It was found that dhp and the synergistic carbonate are non-competitive binders. Based on the stability constants obtained for V(IV)O-apoTf complexes and estimated for V(IV)O-HSA (= human serum albumin), modeling calculations were performed on the distribution of V(IV)O among the components of blood serum. The results were confirmed by HPLC-ICP-MS (liquid chromatography-inductively coupled plasma spectroscopy-mass spectrometry) measurements. The ex vivo interactions of the V(IV)O complexes formed with mal, picolinic acid (pic) and dhp with serum protein standards and also with human serum samples were evaluated. The proteins were firstly separated by (HPLC), and the V content of each fraction was determined by ICP-MS. All the studied V(IV)O compounds displayed similar chromatographic profiles, associated almost exclusively with apotransferrin as predicted by the modeling calculations. Under physiological conditions, the interactions with HSA of all of the species under study were negligible. Therefore Tf seems to be the main V(IV)O transporter in the serum under in vitro conditions, and this association is practically independent of the chemical form in which V(IV)O is administered.
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