Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Selenium Compounds”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 955 records · Page 53Linked to original sources
PubMed1998

Quantum dot bioconjugates for ultrasensitive nonisotopic detection.

Highly luminescent semiconductor quantum dots (zinc sulfide-capped cadmium selenide) have been covalently coupled to biomolecules for use in ultrasensitive biological detection. In comparison with organic dyes such as rhodamine, this class of luminescent labels is 20 times as bright, 100 times as stable against photobleaching, and one-third as wide in spectral linewidth. These nanometer-sized conjugates are water-soluble and biocompatible. Quantum dots that were labeled with the protein transferrin underwent receptor-mediated endocytosis in cultured HeLa cells, and those dots that were labeled with immunomolecules recognized specific antibodies or antigens.

Cadmium Compounds↗
PubMed1986

Selenium yeast.

Baker's yeast is able to assimilate carbon, nitrogen, phosphorus and sulphur sources together with a great number of minerals and trace elements into a palatable, nutritious product. The metabolism of yeast is precisely controlled during the production growth phase and thus it is possible to determine the composition of the product by controlling the raw materials. Because of existing deficiencies in the availability of certain trace elements, mainly selenium, in Finnish diets, we started testing the possibilities for enriching yeast with this essential trace element about five years ago. We have succeeded in developing a special yeast product with a selenium concentration of 500 mg/kg dry matter. Selenium was expected, because of its structural similarity to sulphur, to replace sulphur in the biosynthetic reactions of the yeast cell. We have recently studied the incorporation and distribution of selenium in yeast with radioactive selenium (75Se). Analysis of the protein fraction of selenium yeast has shown that selenium is present in all the major soluble proteins. Selenomethionine was identified as the major selenium-containing compound in the protein fraction as well as in the whole cell.

Amino Acids↗
PubMed2004

Methanococcus vannielii selenium metabolism: purification and N-terminal amino acid sequences of a novel selenium-binding protein and selenocysteine lyase.

Selenium is an essential component of several enzymes and proteins in a number of methane-producing archae. Information concerning accessory proteins that function in selenium transport processes, however, is limited. A novel selenium-binding protein with a potential transport role and a selenocysteine lyase that serves as a selenium delivery protein are present in Methanococcus vannielii. The selenium-binding protein was purified from extracts of 75Se-labeled cells. Although there was gradual loss of 75Se during purification, the isolated protein still could be detected as a radioactive 42 kDa species on native PAGE gels and as a 33 kDa species on SDS PAGE gels. The N-terminal amino acid sequence of residues 1 - 63 of the protein was determined by automated Edman degradative analysis. The only homologous sequence detected in the recorded data base was that of a gene encoding an unknown protein located in the genomic sequence of Methanococcus maripaludis. Cloning and expression of the corresponding gene from M. vannielii are described in a manuscript in press (Self et al.). A 47 kDa selenocysteine lyase isolated from M. vannielii extracts exhibited sequence homology to the NIFS family of proteins that transport sulfur. The purified selenocysteine lyase catalyzed the elimination of an elemental form of selenium from free selenocysteine and delivered this selenium directly to selenophosphate synthetase. The synthetase converted the selenium to selenophosphate in an ATP-dependent reaction.

Amino Acid Sequence↗
PubMed2004

Fluorescence resonance energy transfer between quantum dot donors and dye-labeled protein acceptors.

We used luminescent CdSe-ZnS core-shell quantum dots (QDs) as energy donors in fluorescent resonance energy transfer (FRET) assays. Engineered maltose binding protein (MBP) appended with an oligohistidine tail and labeled with an acceptor dye (Cy3) was immobilized on the nanocrystals via a noncovalent self-assembly scheme. This configuration allowed accurate control of the donor-acceptor separation distance to a range smaller than 100 A and provided a good model system to explore FRET phenomena in QD-protein-dye conjugates. This QD-MBP conjugate presents two advantages: (1) it permits one to tune the degree of spectral overlap between donor and acceptor and (2) provides a unique configuration where a single donor can interact with several acceptors simultaneously. The FRET signal was measured for these complexes as a function of both degree of spectral overlap and fraction of dye-labeled proteins in the QD conjugate. Data showed that substantial acceptor signals were measured upon conjugate formation, indicating efficient nonradiative exciton transfer between QD donors and dye-labeled protein acceptors. FRET efficiency can be controlled either by tuning the QD photoemission or by adjusting the number of dye-labeled proteins immobilized on the QD center. Results showed a clear dependence of the efficiency on the spectral overlap between the QD donor and dye acceptor. Apparent donor-acceptor distances were determined from efficiency measurements and corresponding Förster distances, and these results agreed with QD bioconjugate dimensions extracted from structural data and core size variations among QD populations.

Cadmium Compounds↗
PubMed2005

Fluorescence resonance energy transfer in CdSe/ZnS-DNA conjugates: probing hybridization and DNA cleavage.

Nucleic-acid-functionalized CdSe/ZnS quantum dots (QDs) were hybridized with the complementary Texas-Red-functionalized nucleic acid. The hybridization was monitored by following the fluorescence resonance energy transfer from the QDs to the dye units. Treatment of the QD/dye DNA duplex structure with DNase I resulted in the cleavage of the DNA and the recovery of the fluorescence properties of the CdSe/ZnS QDs. The luminescence properties of the QDs were, however, only partially recovered due to the nonspecific adsorption of the dye onto the QDs. Similarly, nucleic-acid-functionalized Au nanoparticles (Au NPs) were hybridized with the complementary Texas-Red-labeled nucleic acid. The hybridization was followed by the fluorescence quenching of the dye by the Au NPs. Treatment of the Au NP/dye DNA duplex with DNase I resulted in the cleavage of the DNA and the partial recovery of the dye fluorescence. The incomplete recovery of the dye fluorescence originated from the nonspecific binding of the dye units to the Au NPs. The nonspecific binding of the dye to the CdSe/ZnS QDs and the Au NPs is attributed to nonprotected surface vacancies in the two systems.

Base Sequence↗
PubMed2006

Photoinduced charge transfer and efficient solar energy conversion in a blend of a red polyfluorene copolymer with CdSe nanoparticles.

We present measurements of charge transfer and the photovoltaic effect in a blend of the alternating polyfluorene copolymer poly(2,7-(9,9-dioctyl-fluorene)-alt-5,5-(4',7'-di-2-thienyl-2',1',3'-benzothiadiazole)) with branched CdSe nanoparticles. Quasi-steady-state photoinduced absorption measurements identified a long-lived charged species that formed after photoexcitation at room temperature. Photovoltaic devices based on this blend system showed a spectral response extending to 650 nm and gave a solar power conversion efficiency of 2.4% under Air Mass 1.5 Global (AM1.5G) conditions.

Cadmium Compounds↗
PubMed2004

Dimethylselenide demethylation is an adaptive response to selenium deprivation in the archaeon Methanococcus voltae.

The archaeon Methanococcus voltae needs selenium for optimal growth. A gene group most likely involved in the demethylation of dimethylselenide was discovered, the expression of which is induced upon selenium deprivation. The operon comprises open reading frames for a corrinoid protein and two putative methyltransferases. It is shown that the addition of dimethylselenide to selenium-depleted growth medium relieves the lack of selenium, as indicated by the repression of a promoter of a transcription unit encoding selenium-free hydrogenases which is normally active only upon selenium deprivation. Knockout mutants of the corrinoid protein or one of the two methyltransferase genes did not show repression of the hydrogenase promoter in the presence of dimethylselenide. The mutation of the other methyltransferase gene had no effect. Growth rates of the two effective mutants were reduced compared to wild-type cells in selenium-limited medium in the presence of dimethylselenide.

Adaptation, Physiological↗
PubMed2005

HAADF imaging: an effective technique for the study of nonhomogeneous nanostructures.

Atomic number contrast (Z-contrast) imaging using high-angle annular dark field (HAADF) detector, along with high resolution electron microscopy (HREM), is used to study the nanostructured metal, semiconductor, mixed oxide, and soft matter composites of inhomogeneous nature. A comparison between the HREM and HAADF images for the analysis of crystal structure, defects, and compositional inhomogenity in those nanostructures has been made. While the HREM technique is efficient in determining bulk crystallinity and defect structures, the HAADF imaging technique is superior in determining the surface inhomogenity, defect structures in the interior of the nanostructures, even at atomic resolution. The efficiency of the HAADF imaging technique in determining the surface inhomogenity and defect structures is demonstrated for the Au-Pt bimetallic clusters, CdSe nanofibers and nanowires, Nb16W18O94 mixed oxide, and polystyrene-mormorillonite clay nanocomposites.

Cadmium Compounds↗
PubMed2005

Bioremediation potential of a perchlorate-enriched sewage sludge consortium.

The purpose of this work was to explore the reductive bioremediation potential of a perchlorate-enriched facultative anaerobic consortium. Rapid perchlorate reduction and bacterial growth were observed up to 1.84 g l(-1) of perchlorate, but not at 3.82 g l(-1) due to the toxicity. The specific growth rate of the mixed consortium was 0.1 h(-1). The consortium co-reduced perchlorate and nitrate with acetate as e- donor and carbon source. The presence of nitrate slowed down the perchlorate reduction rate. The other e- acceptors utilized include oxygen, chlorate, Cr(VI), and selenate. Over 95% of the 16 mg l(-1) of added Cr(VI) was reduced within 24 h of incubation with a high-density perchlorate-grown consortium. However, the consortium failed to couple growth with reduction of nitrite, sulfate, thiosulfate, and sulfite. During the search for autotrophic perchlorate reduction, many consortia from very diverse natural sources could not use sulfur compounds such as thiosulfate as e- donor.

Bacteria, Anaerobic↗
PubMedDate not supplied

Effect of selenium on distribution, demethylation, and excretion of methylmercury by the guinea pig.

The influence of selenium on methylmercury excretion, organ and subcellular distribution, and demethylation was studied in the guinea pig at different times following a single equimolar dose (50 miroM/kg) of CH203 3) HgCl and Na2SeO3 administered separately or concomitantly per os. Excretion of mercury through feces was the dominant clearance pathway in both groups. Selenium significantly decreased excretion of total and organic mercury in feces during the course of the study, but in the urine only on d 13. Selenium also significantly decreased the concentration of total mercury in major organs. The exception was brain on d 1, in which mercury levels were higher in the presence of selenium; however, on d 7 and 13 both cerebrum and cerebellum showed lower mercury levels as compared to the group treated with methylmercury alone. Selenium had no significant effect on the subcellular mercury distribution in the liver, kidney, and cerebrum, other than that which could be accounted for the whole organ uptake. The level of organic mercury in most of the analyzed organs was significantly decreased by the presence of selenium; however, relative proportions of inorganic to organic mercury remain unchanged. The single exception was kidney, where selenium markedly decreased the relative amount of inorganic mercury.

Animals↗
PubMed1989

Tissue selenium levels in selenium-supplemented rats and their relevance in mammary cancer protection.

The present study was designed to investigate whether there is any correlation between the anticarcinogenic efficacy of selenium (Se) compounds and tissue Se retention under high levels of supplementation. With the use of the dimethylbenz[a]anthracene-induced mammary tumor model in chemoprevention experiments, our data showed that selenomethionine was not as active as selenite over a graded dose range from 1 to 5 p.p.m. Se. Tissue Se concentrations in blood, liver, kidney and skeletal muscle were always higher in rats given selenomethionine compared with those given selenite at each of the three levels tested (1, 3 and 5 p.p.m. Se). The difference was only minimal in blood, but became more pronounced in the liver and kidney, and was quite dramatic in the skeletal muscle. Thus a high tissue concentration or total body burden of Se is not necessarily an indicator of reduced susceptibility to carcinogenesis. The bioavailability of the Se pool in maintaining liver glutathione peroxidase activity during a period of Se deprivation, following excess selenite or selenomethionine loading, was also assessed. The half-life of decay of the enzyme was calculated to be 4.2 and 9.1 days respectively, in those rats that had already been exposed to 3 p.p.m. Se as either selenite or selenomethionine. From a nutritional viewpoint, selenomethionine may be superior to selenite, especially with respect to maintenance of glutathione peroxidase during periods of Se inadequacy, but the reverse seems to be true in terms of anticarcinogenic potency under high levels of Se supplementation. These results suggest that the nutritional and anticarcinogenic efficacies of a given Se compound may not be parallel to each other.

9,10-Dimethyl-1,2-benzanthracene↗
PubMedDate not supplied

Selenalysine as substrate of lysine decarboxylase.

Selenalysine, a lysine analog having the C4 methylene group substituted by a selenium atom, may be decarboxylated to selenolanthionamine by bacterial lysine decarboxylase. The kinetic parameters obtained studying comparatively the decarboxylation of lysine, thialysine and selenalysine showed that while the enzyme is more effective on lysine than on its two analogs, there are no great differences between the last two. These results indicate that the substrate specificity of lysine decarboxylase is greatly affected by the substitution of a carbon atom of the substrate molecule, but the presence of either sulfur or selenium as eteroatom is without appreciable effect on the binding of the lysine analogs to the enzyme. In other words either sulfur- or selenium-containing substrate analogs are acted upon in the same way by lysine decarboxylase.

Carboxy-Lyases↗