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PubMed1992

Elemental speciation by liquid chromatography-inductively coupled plasma mass spectrometry with direct injection nebulization.

A new version of the direct injection nebulizer (DIN) is used to interface liquid chromatographic (LC) separations with element-selective detection using inductively coupled plasma mass spectrometry (ICP-MS). The DIN injects all of the sample into the ICP and has a dead volume of less than 1 microliter. Charged species of arsenic and tin are separated as ion pairs on a micro-scale (1 mm i.d.), packed, reversed-phase column. Detection limits are 0.2-0.6 pg for arsenic and 8-10 pg for tin. For methanol + water eluents, the signal is highest at 25% methanol and stays within 25% of this maximum as the methanol fraction is varied from 20 to 80%. Compared with LC-ICP-MS with conventional nebulizers, the absolute detection limits and chromatographic resolution are substantially superior, and the dependence of analyte signal on solvent composition is somewhat less severe with the DIN.

Arsenicals↗
PubMed2004

Organotins in marine mammals and seabirds from Norwegian territory.

An increasing number of studies indicate that marine mammals and some seabirds are exposed to organotins. However, results from northern and Arctic areas are few. Here results from analysis of tributyltin (TBT), dibutyltin (DBT), monobutyltin (MBT), triphenyltin (TPhT), diphenyltin (DPhT) and monophenyltin (MPhT) in harbour porpoise (Phocoena phocoena), common seal (Phoca vitulina), ringed seal (Phoca hispida) and glaucous gull (Larus hyperboreus) from Norwegian territory are presented. Relatively high concentrations of DBT, TBT and MBT were observed in muscle, kidney and liver from harbour porpoises caught in northern Norway in 1988, just before restrictions on the use of tributyltin (TBT)(mainly on small boats) were introduced in several European countries. The concentrations in harbour porpoise muscle tissue were reduced significantly 11 years later, possibly as a result of the introduced restrictions. Considerably lower concentrations of butyltins were observed in the seals compared to porpoises. The lowest levels of organotins were found in ringed seals from Spitsbergen, where only traces of dibutyltin (DBT) and monobutyltin (MBT) were observed. Traces of DBT and MBT were also found in some individual glaucous gulls from Bear Island. The sum of the degradation products MBT and DBT in liver samples from all analysed species were generally higher than TBT itself. Triphenyltin (TPhT) was observed in all porpoise samples and in livers of common seals. Also the sum of the degradation products MPhT and DPhT in liver samples from porpoise and common seals were higher than TPhT. No traces of phenyltins were found in ringed seals from Spitsbergen or in glaucous gulls from Bear Island. The limited data available indicate low to moderate exposure to organotins in northern areas (Spitsbergen and Bear Island). Marine mammals are however more exposed further south along the Norwegian Coast.

Animals↗
PubMed2004

Liquid chromatography-hydride generation-atomic absorption spectrometry for the speciation of tin in seafoods.

Liquid chromatography with hydride generation atomic absorption spectrometry as the detection system was applied to the separation and determination of inorganic tin, tributyltin, dibutyltin, monobutyltin, diphenyltin and monophenyltin. A reversed phase C18 column and a methanol/water/acetic acid (70:27:3, v/v/v) mixture containing 0.05%(v/v) triethylamine and 0.1%(w/v) tropolone as the mobile phase (isocratic elution) were used. Extraction of organotins from the samples was carried out using methanol containing 0.05%(w/v) tropolone, a process that was repeated twice. The supernatants were shaken with water and dichloromethane in a separating funnel and the organic phase was collected and evaporated to dryness. When the method was applied to the speciation of tin in fresh and canned mussels, no organotins above the detection limits were identified in any of the samples, inorganic tin being the only species detected. The reliability of the procedure was checked by analyzing the total tin content of the samples by electrothermal atomic absorption spectrometry and by speciation of tin in a certified reference material, mussel tissue (CRM 477). The method can be used for environmental monitoring of organotins contaminated samples.

Chromatography, Liquid↗
PubMed2005

Synthesis of a pH dependent covalent imprinted polymer able to recognize organotin species.

The covalent imprinting approach has for the first time been successfully applied for the synthesis of an imprinted polymer able to recognize organotin species. The synthesis has been accomplished by co-polymerization of the complex Bu(2)SnO-m-vinylbenzoin as the imprinting template plus co-monomer sodium methacrylate, and ethylene glycol dimethacrylate as cross-linker. The imprinting effect has been evidenced within the narrow pH range 2.5< pH< 3.5. At lower pH values, the imprinting effect is prevented by the exclusive existence of non-specific interactions, whereas pH>3.5 provokes a strong rebind of the template in both imprinted and non-imprinted polymers. This pH dependency can be explained as a selective chemical modification which reduces bind diversity following a model based on enolization by protonation of the specific cavities. Characterization of the adsorption isotherms showed good agreement with the Langmuir-Freundlich (LF) model, presenting quite homogeneous binding sites for a bulk material and high capacity in the imprinting pH range. In addition, the affinity spectrum (AS) method has been represented showing the typical profiles of LF isotherm for both sub-saturation and saturation levels, being in general agreement with the encountered values for fitting coefficients. The covalent molecular imprinted polymer has been successfully evaluated in a SPE process for further OTC determination in the certified mussel tissue (CRM 477).

Adsorption↗
PubMed1982

Studies on the nature of the high-affinity trialkyltin binding site of rat liver mitochondria.

1. The proteolipid fraction isolated from rat liver mitochondria pretreated with [3H]triphenyltin chloride is enriched in triphenyltin compared with the original mitochondria. 2. Part of this [3H]triphenyltin is eluted with a protein of Mr 5000-6000 on Sephadex LH20 chromatography. 2. Mössbauer spectra of the proteolipid fraction treated with 119Sn-enriched triethyltin chloride show a doublet which corresponds closely with that assigned previously [Farrow & Dawson (1978) Eur. J. Biochem. 86. 85-95] to the absorption of triethyltin bound to the high-affinity binding site of the mitochondrial ATPase.

Animals↗
PubMed1996

Interaction of dibutyltin-3-hydroxyflavone bromide with the 16 kDa proteolipid indicates the disposition of proton translocation sites of the vacuolar ATPase.

The organotin complex dibutyltin-3-hydroxyflavone bromide [Bu2Sn(of)Br] has been shown to bind to the 16 kDa proteolipid of Nephrops norvegicus, either in the form of the native protein or after heterologous expression in Saccharomyces and assembly into a hybrid vacuolar H(+)-ATPase. Titration of Bu2Sn(of)Br against the 16 kDa proteolipid results in a marked fluorescence enhancement, consistent with binding to a single affinity site on the protein. Vacuolar ATPase-dependent ATP hydrolysis was also inhibited by Bu2Sn(of)Br, with the inhibition constant correlating well with dissociation constants determined for binding of Bu2Sn(of)Br complex to the proteolipid. The fluorescence enhancement produced by interaction of probe with proteolipid can be back-titrated by dicyclohexylcarbodiimide (DCCD), which covalently modifies Glu140 on helix-4 of the polypeptide. Expression of a mutant proteolipid in which Glu140 was changed to a glycine resulted in assembly of a vacuolar ATPase which was inactive in proton pumping and which had reduced ATPase activity. Co-expression studies with this mutant and wild-type proteolipids suggest that proton pumping can only occur in a vacuolar ATPase containing exclusively wild-type proteolipid. The fluorescent enhancement of affinity of Bu2Sn(of)Br for the mutant proteolipid was not significantly altered, with the organotin complex having no effect on residual ATPase activity. Interaction of the probe with mutant proteolipid was unaffected by DCCD. These data suggest an overlap in the binding sites of organotin and DCCD, and have implications for the organization and structure of proton-translocating pathways in the facuolar H(+)-ATPase.

Adenosine Triphosphate↗
PubMed1996

Triphenyltin chloride induces glucose intolerance by the suppression of insulin release from hamster pancreatic beta-cells.

UNLABELLED: We performed an intravenous glucose tolerance test (IVGTT) after the administration of triphenyltin chloride (TPTCl-Ad) in hamsters in order to confirm the presence of glucose intolerance and to clarify the pathogenesis of TPTCl-induced glucose intolerance. On the 1st, 2nd, 3rd, 4th and 7th days after TPTCl-Ad or the administration of sesame oil alone as a control, glucose was injected at a dose of 0.05 g glucose/100 g B.W., and then PG, IRI and TG were measured on 0, 1, 2, 3, 5 and 10 min after IVGTT. The TPT concentration in the pancreas was measured by gaschromatography and the morphological findings with a transmission electron microscope were compared between the TPTCl-Ad and the control hamsters. FPG on the 1st and the 2nd days after TPTCl-Ad were significantly higher than those in control, but those on the 4th and the 7th day recovered up to the control level. In contrast, basal IRI levels showed reciprocal results compared to the FPG levels. delta IRI/ delta PG on the 1st day after TPTCl-Ad was significantly reduced compared to the control. Fasting TG on the 1st day after TPTCl-Ad was much higher than the control. TPT-concentration on the 1st day after TPTCl-Ad showed peak values and its concentration gradually decreased. Electron microscopic findings in the pancreas after TPTCl-Ad indicated neither destruction nor lymphocyte infiltration of the pancreas. CONCLUSIONS: The present data suggest that the administration of TPTCl in hamsters induces a functional transient damage on islet cells but not a morphological disorder, which shows an essentially different nature from the change in the pancreas induced by viral infection or by a large amount of streptozotocin.

Animals↗
PubMed2004

Biodistribution and pharmacokinetics of variously molecular sized 117mSn(II)-polyethyleneiminomethyl phosphonate complexes in the normal primate model as potential selective therapeutic bone agents.

In the search for a cure for metastatic bone cancer, 117mSn with its conversion electrons and low energy photons both of discrete energies shows little bone marrow toxicity, providing the opportunity to increase the administered dose. Selective accumulation in lesions would capitalise on this advantage. The 10-30 kDa fraction of the water-soluble polymer polyethyleneimine, functionalised with methyl phosphonate groups (PEI-MP) and labelled with 99mTc, has shown selective uptake into bone tumours. Furthermore using speciation calculations it was predicted that the Sn(II)-PEI-MP complex would remain intact in the blood plasma. Because of this positive indication animal experiments were carried out to test this prediction. This paper relates the labelling, biodistribution and pharmacokinetics of various fractions of 117mSn-(II) PEI-MP in the normal primate model, and points to promising therapeutic possibilities.

Animals↗