Academic literature on the topic 'Iron proteins – Analysis'

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Journal articles on the topic "Iron proteins – Analysis"

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Prasannavadhana, A., Santosh Kumar, Prasad Thomas, Laxmi Narayan Sarangi, Santosh Kumar Gupta, Adyasha Priyadarshini, Viswas Konasagara Nagaleekar, and Vijendra Pal Singh. "Outer Membrane Proteome Analysis of Indian Strain ofPasteurella multocidaSerotype B:2 by MALDI-TOF/MS Analysis." Scientific World Journal 2014 (2014): 1–10. http://dx.doi.org/10.1155/2014/617034.

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Identification of outer membrane proteins (OMPs) is important to understand the bacteria structure and function, host-pathogen interaction, development of novel vaccine candidates, and diagnostic antigens. But till now the key antigens ofP. multocidaB:2 isolate causing haemorrhagic septicaemia (HS) in animals are not clearly defined. In this study, P52 strain ofP. multocidaserotype B:2 was grownin vitrounder iron-rich and iron-limited condition. The OMPs were extracted by sarkosyl method followed by SDS-PAGE and the proteins were identified by MALDI-TOF/MS analysis. In total, 22 proteins were identified, of which 7 were observed exclusively under iron-limited condition. Most of the high molecular weight proteins (TbpA, HgbA, HgbB, HasR, IroA, and HemR) identified in this study were involved in iron acquisition. Some hypothetical proteins (HP-KCU-10206, HP and AAUPMB 08244, HP AAUPMB 21592, HP AAUPMB 19766, AAUPMB 11295) were observed for the first time in this study which could be unique to serotype B:2. Further functionalin vivostudy of the proteins identified are required to explore the utility of these proteins in developing diagnostics and vaccine against HS.
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Azman, Adleen, Kalidasan Vasodavan, Narcisse Joseph, Suresh Kumar, Rukman A. Hamat, Syafinaz A. Nordin, Wan M. Aizat, Alex van Belkum, and Vasantha K. Neela. "Physiological and proteomic analysis of Stenotrophomonas maltophilia grown under the iron-limited condition." Future Microbiology 14, no. 16 (November 2019): 1417–28. http://dx.doi.org/10.2217/fmb-2019-0174.

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Aims: To study physiological and proteomic analysis of Stenotrophomonas maltophilia grown under iron-limited condition. Methods: One clinical and environmental S. maltophilia isolates grown under iron-depleted conditions were studied for siderophore production, ability to kill nematodes and alteration in protein expression using isobaric tags for relative and absolute quantification (ITRAQ). Results & conclusions: Siderophore production was observed in both clinical and environmental strains under iron-depleted conditions. Caenorhabditis elegans assay showed higher killing rate under iron-depleted (96%) compared with normal condition (76%). The proteins identified revealed, 96 proteins upregulated and 26 proteins downregulated for the two isolates under iron depletion. The upregulated proteins included several iron acquisition proteins, metabolic proteins and putative virulence proteins.
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Petrak, Jiri, Denisa Myslivcova, Petr Man, Radek Cmejla, Jana Cmejlova, and Daniel Vyoral. "Proteomic analysis of iron overload in human hepatoma cells." American Journal of Physiology-Gastrointestinal and Liver Physiology 290, no. 5 (May 2006): G1059—G1066. http://dx.doi.org/10.1152/ajpgi.00469.2005.

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Iron-mediated organ damage is common in patients with iron overload diseases, namely, hereditary hemochromatosis. Massive iron deposition in parenchymal organs, particularly in the liver, causes organ dysfunction, fibrosis, cirrhosis, and also hepatocellular carcinoma. To obtain deeper insight into the poorly understood and complex cellular response to iron overload and consequent oxidative stress, we studied iron overload in liver-derived HepG2 cells. Human hepatoma HepG2 cells were exposed to a high concentration of iron for 3 days, and protein expression changes initiated by the iron overload were studied by two-dimensional electrophoresis and mass spectrometry. From a total of 1,060 spots observed, 21spots were differentially expressed by iron overload. We identified 19 of them; 11 identified proteins were upregulated, whereas 8 identified proteins showed a decline in response to iron overload. The differentially expressed proteins are involved in iron storage, stress response and protection against oxidative stress, protein folding, energy metabolism, gene expression, cell cycle regulation, and other processes. Many of these molecules have not been previously suggested to be involved in the response to iron overload and the consequent oxidative stress.
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Liu, MaFeng, Mi Huang, DeKang Zhu, MingShu Wang, RenYong Jia, Shun Chen, KunFeng Sun, et al. "Identifying the Genes Responsible for Iron-Limited Condition in Riemerella anatipestifer CH-1 through RNA-Seq-Based Analysis." BioMed Research International 2017 (2017): 1–10. http://dx.doi.org/10.1155/2017/8682057.

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One of the important elements for most bacterial growth is iron, the bioavailability of which is limited in hosts. Riemerella anatipestifer (R. anatipestifer, RA), an important duck pathogen, requires iron to live. However, the genes involved in iron metabolism and the mechanisms of iron transport are largely unknown. Here, we investigated the transcriptomic effects of iron limitation condition on R. anatipestifer CH-1 using the RNA-Seq and RNA-Seq-based analysis. Data analysis revealed genes encoding functions related to iron homeostasis, including a number of putative TonB-dependent receptor systems, a HmuY-like protein-dependent hemin (an iron-containing porphyrin) uptake system, a Feo system, a gene cluster related to starch utilization, and genes encoding hypothetical proteins that were significantly upregulated in response to iron limitation. Compared to the number of upregulated genes, more genes were significantly downregulated in response to iron limitation. The downregulated genes mainly encoded a number of outer membrane receptors, DNA-binding proteins, phage-related proteins, and many hypothetical proteins. This information suggested that RNA-Seq-based analysis in iron-limited medium is an effective and fast method for identifying genes involved in iron uptake in R. anatipestifer CH-1.
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Schryvers, Anthony B., and B. Craig Lee. "Analysis of bacterial receptors for host iron-binding proteins." Journal of Microbiological Methods 18, no. 3 (October 1993): 255–66. http://dx.doi.org/10.1016/0167-7012(93)90040-o.

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Cullen, Paul A., Stuart J. Cordwell, Dieter M. Bulach, David A. Haake, and Ben Adler. "Global Analysis of Outer Membrane Proteins from Leptospira interrogans Serovar Lai." Infection and Immunity 70, no. 5 (May 2002): 2311–18. http://dx.doi.org/10.1128/iai.70.5.2311-2318.2002.

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ABSTRACT Recombinant leptospiral outer membrane proteins (OMPs) can elicit immunity to leptospirosis in a hamster infection model. Previously characterized OMPs appear highly conserved, and thus their potential to stimulate heterologous immunity is of critical importance. In this study we undertook a global analysis of leptospiral OMPs, which were obtained by Triton X-114 extraction and phase partitioning. Outer membrane fractions were isolated from Leptospira interrogans serovar Lai grown at 20, 30, and 37°C with or without 10% fetal calf serum and, finally, in iron-depleted medium. The OMPs were separated by two-dimensional gel electrophoresis. Gel patterns from each of the five conditions were compared via image analysis, and 37 gel-purified proteins were tryptically digested and characterized by mass spectrometry (MS). Matrix-assisted laser desorption ionization-time-of-flight MS was used to rapidly identify leptospiral OMPs present in sequence databases. Proteins identified by this approach included the outer membrane lipoproteins LipL32, LipL36, LipL41, and LipL48. No known proteins from any cellular location other than the outer membrane were identified. Tandem electrospray MS was used to obtain peptide sequence information from eight novel proteins designated pL18, pL21, pL22, pL24, pL45, pL47/49, pL50, and pL55. The expression of LipL36 and pL50 was not apparent at temperatures above 30°C or under iron-depleted conditions. The expression of pL24 was also downregulated after iron depletion. The leptospiral major OMP LipL32 was observed to undergo substantial cleavage under all conditions except iron depletion. Additionally, significant downregulation of these mass forms was observed under iron limitation at 30°C, but not at 30°C alone, suggesting that LipL32 processing is dependent on iron-regulated extracellular proteases. However, separate cleavage products responded differently to changes in growth temperature and medium constituents, indicating that more than one process may be involved in LipL32 processing. Furthermore, under iron-depleted conditions there was no concomitant increase in the levels of the intact form of LipL32. The temperature- and iron-regulated expression of LipL36 and the iron-dependent cleavage of LipL32 were confirmed by immunoblotting with specific antisera. Global analysis of the cellular location and expression of leptospiral proteins will be useful in the annotation of genomic sequence data and in providing insight into the biology of Leptospira.
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Carey-Fung, Oscar, Jesse T. Beasley, and Alexander A. T. Johnson. "Annotation and Molecular Characterisation of the TaIRO3 and TaHRZ Iron Homeostasis Genes in Bread Wheat (Triticum aestivum L.)." Genes 12, no. 5 (April 27, 2021): 653. http://dx.doi.org/10.3390/genes12050653.

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Effective maintenance of plant iron (Fe) homoeostasis relies on a network of transcription factors (TFs) that respond to environmental conditions and regulate Fe uptake, translocation, and storage. The iron-related transcription factor 3 (IRO3), as well as haemerythrin motif-containing really interesting new gene (RING) protein and zinc finger protein (HRZ), are major regulators of Fe homeostasis in diploid species like Arabidopsis (Arabidopsis thaliana) and rice (Oryza sativa L.), but remain uncharacterised in hexaploid bread wheat (Triticum aestivum L.). In this study, we have identified, annotated, and characterised three TaIRO3 homoeologs and six TaHRZ1 and TaHRZ2 homoeologs in the bread wheat genome. Protein analysis revealed that TaIRO3 and TaHRZ proteins contain functionally conserved domains for DNA-binding, dimerisation, Fe binding, or polyubiquitination, and phylogenetic analysis revealed clustering of TaIRO3 and TaHRZ proteins with other monocot IRO3 and HRZ proteins, respectively. Quantitative reverse-transcription PCR analysis revealed that all TaIRO3 and TaHRZ homoeologs have unique tissue expression profiles and are upregulated in shoot tissues in response to Fe deficiency. After 24 h of Fe deficiency, the expression of TaHRZ homoeologs was upregulated, while the expression of TaIRO3 homoeologs was unchanged, suggesting that TaHRZ functions upstream of TaIRO3 in the wheat Fe homeostasis TF network.
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Kucera, Jiri, Eva Pakostova, Oldrich Janiczek, and Martin Mandl. "Changes in Acidithiobacillus ferrooxidans Ability to Reduce Ferric Iron by Elemental Sulfur." Advanced Materials Research 1130 (November 2015): 97–100. http://dx.doi.org/10.4028/www.scientific.net/amr.1130.97.

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Ferric iron may act as a thermodynamically favourable electron acceptor during elemental sulfur oxidation byAcidithiobacillus ferrooxidansin extremely acidic anoxic environments. A loss of anaerobic ferric iron reduction ability has been observed in ferrous iron-grownA. ferrooxidansCCM 4253 after aerobic passaging on elemental sulfur. In this study, iron-oxidising cells aerobically adapted from ferrous iron to elemental sulfur were still able to anaerobically reduce ferric iron, however, following aerobic passage on elemental sulfur it could not. Preliminary quantitative proteomic analysis of whole cell lysates of the passage that lost anaerobic ferric iron-reducing activity resulted in 150 repressed protein spots in comparison with the antecedent culture, which retained the activity. Identification of selected protein spots by tandem mass spectrometry revealed physiologically important proteins including rusticyanin and outer-membrane cytochrome Cyc2, which are involved in iron oxidation. Other proteins were associated with sulfur metabolism such as sulfide-quinone reductase and proteins encoded by the thiosulfate dehydrogenase and heterodisulfide reductase complex operons. Furthermore, proteomic analysis identified proteins directly related to anaerobiosis. The results indicate the importance of iron-oxidising system components for anaerobic sulfur oxidation in the studied microbial strain.
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Marchewka, Damian, Irena Roterman, Magdalena Strus, Klaudyna Śpiewak, and Grzegorz Majka. "Structural Analysis of the Lactoferrin Iron Binding Pockets." bams 8, no. 4 (December 2012): 351–59. http://dx.doi.org/10.1515/bams-2012-0024.

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ABSTRACT Lactoferrin (Lf) - member of the transferrin family of proteins responsible for many different functions in the body of mammals participates in regulation of free iron level in the body fluids making the protein bacteriostatic. The main goal of studies was to test the suitability of molecular dynamic simulation to study structural changes in the tertiary structure of lactoferrin. According to ConSurf Server analysis one of the most conservative amino acids was found not only in iron- but also in carbohydrates- binding pockets which may suggest a significant impact of carbohydrates on the functions performed by lactoferrin. Pocket-Finder program applied to find iron-binding pockets revealed the potential Fe binding area. The stability of the ligand deprived protein was verified performing the 50 ns dynamic simulation using the Gromacs program. The tertiary structure changes during the simulation were observed in N-lob solely. No structural changes were observed in C-lob iron-binding pocket.
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Khan, Mateen A. "Analysis of Ion and pH Effects on Iron Response Element (IRE) and mRNA-Iron Regulatory Protein (IRP1) Interactions." Current Chemical Biology 14, no. 2 (November 19, 2020): 88–99. http://dx.doi.org/10.2174/2212796814999200604121937.

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Background: Cellular iron uptake, utilization, and storage are tightly controlled through the action of iron regulatory proteins (IRPs). IRPs achieve this control by binding to IREs-mRNA in the 5'- or 3'-end of mRNAs that encode proteins involved in iron metabolism. The interaction of iron regulatory proteins with mRNAs containing an iron responsive element plays a central role in this regulation. The IRE RNA family of mRNA regulatory structures combines absolutely conserved protein binding sites with phylogenetically conserved base pairs that are specific to each IREs and influence RNA/protein stability. Our previous result revealed the binding and kinetics of IRE RNA with IRP1. The aim of the present study is to gain further insight into the differences in protein/RNA stability as a function of pH and ionic strength. Objective: To determine the extent to which the binding affinity and stability of protein/RNA complex was affected by ionic strength and pH. Methods: Fluorescence spectroscopy was used to characterize IRE RNA-IRP protein interaction. Results: Scatchard analysis revealed that the IRP1 protein binds to a single IRE RNA molecule. The binding affinity of two IRE RNA/IRP was significantly changed with the change in pH. The data suggests that the optimum binding of RNA/IRP complex occurred at pH 7.6. Dissociation constant for two IRE RNA/IRP increased with an increase in ionic strength, with a larger effect for FRT IRE RNA. This suggests that numerous electrostatic interactions occur in the ferritin IRE RNA/IRP than ACO2 IRE RNA/IRP complex. Iodide quenching shows that the majority of the tryptophan residues in IRP1 are solvent-accessible, assuming that most of the tryptophan residues contribute to protein fluorescence. Conclusion: The results obtained from this study clearly indicate that IRE RNA/IRP complex is destabilized by the change in pH and ionic strength. These observations suggest that both pH and ion are important for the assembly and stability of the IRE RNA/IRP complex formation.
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Dissertations / Theses on the topic "Iron proteins – Analysis"

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Ravindranath, Velaga M. "Elucidating the role of mitoferrin (Mfrn), iron regulatory proteins (IRP1 and IRP2) and hephaestin (Heph) in iron metabolism by tagSNP and protein-protein interaction (PPI) analysis." Thesis, London Metropolitan University, 2014. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.639414.

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Precisely how Hephaestin (Heph) facilitate iron release from cells is poorly understood. The work in this thesis tried to establish the role of different iron metabolic proteins, Mitoferrin (Mfrn), IRPs and Heph in iron homeostasis. Analysis of 18 tagSNPs in the Mfrn gene was carried out in an AsianCaucasian population to establish any correlation between the Mfrn tagSNPs, haemoglobin levels and birth weight in the presence of covariates such as sex of the fetus, gestational age and mother's booking weight. Two-way ANCOVA analysis was carried out to check if the covariates have any influence on the dependent variable in the presence of fixed factors. From the ANCOVA analysis of Mfrn tagSN Ps it can be concluded that neither the haemoglobin levels nor the birth weight are dependent on the genotype, fetal sex, nor on their interaction. Owing to the significance in identifying the interacting partners of IRPs and Heph to understand more about their role in iron metabolism, protein-protein interaction studies were also carried out. IRPs and Heph genes were successfully cloned with One-Strep tag. Full length clones were sequence confirmed for any variation after PCR. Before carrying out immunoprecipitation to identify the interacting partners, transfection efficiency, viability and the role of magnetic particles on K562 cells was performed by using IRPs and Heph cloned with One-Strep tag. Lipofectamine-L TX plus transfection had more viable cells and higher efficiency compared with magnetic-assisted transfection . Also, this study confirms that magnetic nanoparticles do not have any adverse or significant effect on IRPs during the transfection. An unsuccessful attempt was made to identify the interacting partners of IRPs and Heph by immunoprecipitation. The current thesis work also involved identification of a potential ferroxidase . Ceruloplasmin (Cp) was used as a postive control. Non-denaturing gel eletrophoresis of the K562, MDA-MB-231 and PNT2-C2 cell fractions confirmed the presence of the extra band establishing the ubiquitous nature of the band. Mass spectrometry analysis identified the excised band as Calreticulin (CALR). This is the first report of calreticulin having ferroxidase activity.
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Lin, Xiaohui, and 林晓晖. "Molecular analysis of an iron transporter gene of Burkholderia speciesMBA4." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2009. http://hub.hku.hk/bib/B4218194X.

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Lin, Xiaohui. "Molecular analysis of an iron transporter gene of Burkholderia species MBA4." Click to view the E-thesis via HKUTO, 2009. http://sunzi.lib.hku.hk/hkuto/record/B4218194X.

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Hook-Barnard, India G. "Molecular analysis of regulatory elements within the escherichia coli fepB leader mRNA." free to MU Campus, others may purchase, 2003. http://wwwlib.umi.com/cr/mo/fullcit?p3091932.

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Jones, Karen Lorraine. "Analysis of ferredoxin and flavodoxin in Anabaena and Trichodesmium using fast protein liquid chromatography." PDXScholar, 1988. https://pdxscholar.library.pdx.edu/open_access_etds/3812.

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Iron is an essential nutrient for growth of photosynthetic microorganisms such as cyanobacteria and algae. Iron is required for proteins involved in the important processes of carbon and nitrogen assimilation. Low concentrations of iron in cultures or natural waters can lead to iron limitation which affects many aspects of algal metabolism. In natural waters, iron limitation can have effects on the patterns and rates of primary productivity. The cellular content of certain proteins can be affected by media iron concentrations. Methods have been used that assay components of the cell as an indirect measure of iron nutritional status. For example, spectroscopy can be performed to determine the cellular concentration of iron-containing proteins involved in photosynthesis. Organisms grown in media that imitate natural conditions, or organisms collected from their natural habitat are usually dilute. Methods that assay iron nutritional status such as spectroscopy and column chromatography require large sample sizes which are difficult to obtain from natural samples. In addition, methods that utilize techniques such as immunology or radioactive labelling are complex and time-consuming. These considerations led to the necessity of developing a technique that would be simple, rapid and effective on dilute samples. The method developed here utilized fast protein liquid chromatography (FPLC), which fulfilled these requirements. A complete analysis could be done within two to three hours with minimal sample treatment. The FPLC was simple to operate and was effective on a sample containing less than 100 μg of protein. Some photosynthetic organisms, when iron-depleted, can produce the flavin-containing protein flavodoxin (Flv). This protein substitutes for the iron-containing protein ferredoxin (Fd) in Fd-dependent reactions such as the light-induced reduction of NADP. The FPLC technique identified and quantified, in relative terms, Fd and Flv in the cell. Optical spectroscopy was used to verify FPLC retention time assignments. The results illustrated how the FPLC could be used to observe the changes in relative Fd and Flv content as a function of media iron concentration in cultures of the cyanobacterium Anabaena grown in the laboratory. It was found that Fd content decreased and Flv content increased with decreasing media iron concentration. In addition, samples of the cyanobacterium Trichodesmium collected from the ocean near Barbados were analyzed using FPLC to assay relative Fd and Flv content. By analogy with Anabaena, Fd and Flv retention times were identified. Using this technique conclusions could be drawn regarding the changing iron nutritional status of Trichodesmium in its natural habitat .
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Martin, Kerri Katherine. "Exploring Metallic Flavor Perception: Analysis of Human Salivary Proteins and the Use of the Iron-Binding Protein Lactoferrin in Reducing Metallic Off-Flavors." Thesis, Virginia Tech, 2012. http://hdl.handle.net/10919/76813.

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Metallic flavors are of concern for many industries including food, health, and water. Metallic off-flavor, induced by ferrous sulfate solution (10mg/L), and its remediation using pre- and post-rinse treatments of water (control) or metal chelators, were studied. Metal chelators included lactoferrin (1 ?M), a natural metal-binding protein in milk and saliva, and EDTA (36 ?M), a synthetic chelator. Time-intensity (TI) evaluation (n=6, 4 female; age 40-70) of lingering metallic flavor indicated that metallic flavor decreased with a post-rinse adjuvant treatment of lactoferrin as indicated by a reduced maximum intensity and area under the curve compared to a pre-rinse treatment; EDTA and water post-rinses were equally effective for three of the TI parameters. Alterations in salivary components were studied in saliva collected (n=8; 5 female, age 40-70) after sipping a lactoferrin solution (1?M) followed with a ferrous sulfate sample (10 mg/ml) to stimulate metallic flavor, as compared to unstimulated whole saliva. Protein concentration, oral lipid oxidation as indicated by thiobarbituric acid reactive substances assay, and iron concentration were determined on individual saliva samples, with no significant differences found between treatments (p>0.05). Protein patterns were qualitatively characterized for each pre-rinse and metallic stimuli from four panelists by two-dimensional gel electrophoresis. A consistent pattern of regions containing major salivary components was observed. This research has shown that lactoferrin protein is a potential natural alternative to synthetic EDTA for reducing iron-induced metallic off-flavors. This study provides a foundation of method development to better understand salivary protein interaction with metals and flavor perception.
Master of Science in Life Sciences
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Gao, Ming. "IDENTIFICATION AND ANALYSIS OF PROTEINS AND GENES RESPONSIBLE FOR MICROBIAL ANAEROBIC NITRATE-DEPENDENT IRON OXIDATION AND OVEREXPRESSION IN E. coli OF PERCHLORATE REDUCTASE." OpenSIUC, 2011. https://opensiuc.lib.siu.edu/dissertations/378.

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SECTION 1 Iron is the fourth most abundant element on the earth crust as well as an essential nutrient for all living organisms. The cycling of iron between the environment and biological systems and the microbial-mediated transformation between Fe2+ and Fe3+ has a significant impact on the biogeochemistry of the environment. The recently discovered microbially-mediated anaerobic nitrate-dependent oxidation of Fe2+ has been shown to play an important role in global iron biogeochemical cycling. Furthermore, the formation of iron oxide from anaerobic nitrate-dependent Fe2+ oxidation results in the adsorption and precipitation of soluble toxic heavy metals and radionuclides from surrounding environment. Therefore, this metabolism has been attracting more and more attention because this process could serve as a cost-effective way to co-remediate nitrate, heavy metals and radionuclides at contaminated sites. Little is known about the molecular genetics of the anaerobic nitrate-dependent Fe2+ oxidation pathway so far. Previous studies in our lab using a microarray approach on Dechloromonas aromatica RCB uncovered the likely involvement of lipoproteins, transmembrane proteins in major operons, cytochromes and signal transduction enzymes in this metabolism. In an effort to further elucidate the metabolic process, a recently isolated bacterium strain Acidovorax ebreus strain TPSY capable of anaerobic nitrate-dependent Fe2+ oxidation was selected as a model organism in this study. By utilizing a 2-dimensional electrophoresis method, a list of candidate proteins which exhibited elevated levels of expression were identified by the comparison of whole cell protein profile between Fe2+-oxidizing strain TPSY cells and control cells. Conserved domain analysis of the protein candidates along with the locus analysis of their corresponding genes revealed two operons (Dtpsy_1460-1463 and Dtpsy_3433-3438) that could encode key components in the anaerobic nitrate-dependent Fe2+ oxidation pathway. An outer membrane efflux pump protein complex encoded by the Dtpsy_1460-1463 operon could play a role in the exportation of periplasmic-accumulated Fe3+ as a detoxification procedure. In addition, a putative ferric reductase protein Dtpsy_3433 and cytochrome reductase-like protein Dtpsy_3436 are likely critical electron transport chain components in this metabolism. Quantitative reverse transcription PCR provided further evidence for the involvement of this operon by demonstrating the transcriptional level up-regulation of the genes in the Dtpsy_3433-3438 operon. This study serves as the first attempt to identify the proteins and genes responsible for anaerobic nitrate-dependent iron oxidation in Acidovorax ebreus strain TPSY. This work has led to the successful identification of a few key proteins and genes responsible for anaerobic nitrate-dependent Fe2+ oxidation, thus providing information important for the elucidation of other components in this electron transport pathway. SECTION 2 Perchlorate is a wide-spread contaminant detected in drinking water and ground water systems in the United States. The current development of a highly sensitive enzymatic bioassay for in situ perchlorate concentration quantification created a need for high-quality and low-cost perchlorate reductase. Perchlorate reductase, originally isolated from DPRB (dissimilatory perchlorate reducing bacteria), is encoded by an operon containing four genes, pcrABCD. Enzymatically active perchlorate reductase purified by traditional methods is composed of two structural subunits, PcrA and PcrB, encoded by the pcrA and pcrB genes, respectively. The lengthy traditional protein purification process and the slow growth rate of DPRB hinder the industrial mass production of this enzyme. In this study, we report an attempt to use E. coli host to overexpress perchlorate reductase and use a polyhistidine tag to enable ease of the subsequent purification. The pcrAB genes encoding the structural subunits of perchlorate reductase were cloned into an expression vector in E. coli. The purification of the recombinant perchlorate reductase was performed under strict anaerobic and denaturing conditions and a highly purified form of the enzyme was obtained. Possible solutions to avoid the formation of inclusion bodies while still maintaining the enzyme activity were discussed. This work proved the feasibility of recombinant perchlorate reductase expression using an E.coli host and the usefulness of the histidine tag in the purification process. In addition, this work provided insights into factors that need to be taken into future consideration in order to obtain the recombinant enzyme with full enzymatic activity. As a final goal, this study will contribute to the development of enzyme-based bioassay for the detection of perchlorate in the environment by lowering the production and purification cost of its key component, the perchlorate reductase.
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Pirani, Parisa. "Surface-Engineered Magnetic Nanoparticles for Sample Preparation and Analysis of Proteins and Peptides." ScholarWorks@UNO, 2015. http://scholarworks.uno.edu/td/2012.

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Sample preparation as an essential step in mass spectrometry-based analysis, plays a critical role in proteomics studies. Magnetic nanoparticles (MNPs) have been widely used in protein and peptide sample preparation due to their magnetic properties, biocompatibility, easy synthesis and surface functionalization. MNPs loaded with analyte or analyte modification reagent can be easily separated from the reaction medium by an externally applied magnetic field. The small size of MNPs provides high analyte loading and extraction capacity. Additionally, MNP can be decorated with different functional groups to achieve selective modification or extraction of analyte. In this study we have utilized silica coated iron oxide magnetic nanoparticles (Fe3O4@SiO2 MNPs) for protein and peptide sample preparation. Fluorescence-based methods were utilized for quantitative and qualitative characterization of N-hydrosucccinimidyl (NHS) ester groups on the surface of Fe3O4@SiO2 MNPs. Fluorophore Dansylcadaverine was conjugated to NHS ester functional groups. Fluorometric measurement of cleaved dansylcadaveine was employed to determine the number of NHS ester groups per MNPs that was found to be 2.6 × 102 and 3.4 × 103for 20 nm and 100 nm Fe3O4@SiO2 MNPrespectively. The efficiency of labeling native bovine serum albumin (BSA) by NHS ester coated Fe3O4@SiO2 MNPs was also explored in terms of maximizing the number of MNPs conjugated per BSA molecule or maximizing the number of BSA molecules conjugated per each MNP. Lysine residues of apolipoprotein B-100 (apoB-100) on the surface of intact human low density lipoprotein (LDL) were labeled by NHS ester modified Fe3O4@SiO2 MNPs in aqueous solvents at room temperature. The MNP labeledapoB-100 was treated by SDS to remove lipids and then digested using trypsin. Tryptic peptides were eluted from MNPs by cleaving disulfide linkage between labeled peptides and MNPs. LC-MS/MS analysis found 28 peptides containing labeled lysine residues. These lysine residues should be on the solvent exposed surface of LDL since the large size of MNPs prevents contact of the labeling reagent to those lysines embedded inside the structure of LDL. TCEP- immobilized Fe3O4@SiO2MNPs were fabricated and utilized for reduction of disulfide bonds in bovine pancreas insulin and two different cyclic peptides. Disulfide bonds were efficiently cleaved at room temperature in both organic and aqueous solvents confirmed by LC-MS/MS analysis of reduced/alkylated protein and peptides. Disulfide reduction and alkylation reactions was performed in one step and the reducing agent was simply separated from peptide and protein solution by magnetic separation.
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DeRocco, Amanda Jean. "Molecular Analysis of Transferrin Binding Protein B in Neisseria Gonorrhoeae." VCU Scholars Compass, 2007. http://scholarscompass.vcu.edu/etd_retro/52.

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The transferrin iron acquisition system of Neisseria consists of two dissimilar proteins, transferrin binding protein A and B (TbpA and TbpB). TbpA and TbpB both specifically and independently bind human transferrin (Tf). TbpA is a TonB-dependent transporter, expression of which is necessary for Tf iron acquisition. In contrast, the lipoprotein TbpB is not necessary for iron internalization; however it makes this process more efficient. The role of TbpB in the transferrin iron acquisition system has not been completely elucidated. It has been suggested that TbpB is entirely surface exposed and tethered to the outer membrane by its lipid moiety. We inserted the hemagluttinin antigen (HA) epitope into TbpB in an effort to examine surface accessible and functional domains of the lipoprotein. We determined that TbpB was entirely surface exposed from just beyond the mature N-terminus. It was previously reported that the N- and C-terminus of TbpB independently bind Tf. HA epitope analysis defined both the N-terminal and C-terminal binding domains. TbpB was previously reported to play an important role in the release of Tf from the receptor. We established that TbpB exhibited a biphasic dissociation pattern; a C-terminal rapid release followed by a slower N-terminal release. These results suggested that the C-terminus plays a role in ligand turnover of the wild-type receptor. Little is known about the transport of TbpB to the outer membrane. In an attempt to identify the signals/mechanisms required for TbpB localization, the signal sequence of the protein was altered. In the absence of lipid modification, TbpB remained associated with the cell, localized to the periplasm. We also noted that internal cysteine residues were not critical for TbpB localization. Our results suggested that TbpB was transported by a lipoprotein-specific mechanism. Additionally, we demonstrated the major outer membrane secretin, PilQ, was not necessary for proper localization of TbpB. The mechanism responsible for this process remains elusive. This body of work represents the first comprehensive study of TbpB topology and function, utilizing the lipoprotein expressed in its native membrane. These results may translate to other, similar lipoprotein receptors of the pathogenic Neisseria, helping to shed light on these poorly understood proteins.
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Al-Saadi, Ali. "Preparation and characterisation of encapsulation magnetic metal iron oxide nanoparticles." Thesis, University of Oxford, 2012. http://ora.ox.ac.uk/objects/uuid:57bdcf38-9d45-48ab-a971-a2d60e2e4391.

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One of the most challenging goals in nanoparticle research is to develop successful protocols for the large-scale, simple and possibly low-cost preparation of morphologically pure nanoparticles with enhanced properties. The work presented in this thesis was focused on the synthesis, characterisation and testing of magnetic nanoparticles and their potential applications. There are a number of magnetic nano-materials prepared for specific applications such as metal oxide nanoparticles encapsulated with various porous materials including Fe₃O₄/Fe₂O₃ coated with soft bio-organic materials such as glycol chitosan and bovine serum albumin and hard materials such as silica (SiO₂) and zinc sulphide (ZnS). The preparation of these materials was achieved principally by bottom-up methods with different approaches including micro-emulsion, precipitation, electrostatic and thermolysis processes. The thesis also presents the uses of various analytical techniques for characterising different types of nano-materials including Attenuated Total Reflection Fourier Transformer Infrared Vibrational Spectroscopy (ATR-FTIR), Ultraviolet Visible- Near Infrared (UV-Vis-NIR) Spectroscopy, Zeta Potentiometric Surface Charge Analysis, Superconducting Quantum Interference Device (SQUID) and Vibration Sample Magnetometry (VSM) for magnetic analysis and powder X-Ray Diffraction (XRD) for crystallographic pattern analysis. There are many applications of magnetic nanoparticles, including nano-carriers for biological and catalytic reagents. The magnetic nanoparticles can facilitate separation in order to isolate the carriers from solution mixtures as compared to many inefficient and expensive classic methods, which include dialysis membrane, electrophoresis, ultracentrifugation, precipitation and column separation methods. There are six key chapters in this thesis: the first chapter introduces the up-to-date literature regarding magnetic nano-materials. The uses of magnetic nano-materials in drug binding and for protein separation are discussed in the second and third chapters. The fourth chapter presents the use of magnetic nanoparticle in conjunction with a photo-catalytic porous overlayer for the photo-catalytic reduction of organic molecules. The fifth chapter describes different analytical techniques used for the characterisation of nanoparticles and the underlying principles and the experimental details are also given. The sixth chapter summarises the results and provides an overview of the work in a wider context of future applications of magnetic nanoparticles.
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Books on the topic "Iron proteins – Analysis"

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Discourses of Ideology and Identity: Social Media and the Iranian Election Protests. Routledge, 2015.

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Book chapters on the topic "Iron proteins – Analysis"

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Crack, Jason C., Jeffrey Green, Andrew J. Thomson, and Nick E. Le Brun. "Techniques for the Production, Isolation, and Analysis of Iron–Sulfur Proteins." In Methods in Molecular Biology, 33–48. Totowa, NJ: Humana Press, 2014. http://dx.doi.org/10.1007/978-1-62703-794-5_4.

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Sherman, Louis A., K. J. Reddy, H. C. Riethman, and George S. Bullerjahn. "Genetic Analysis of a Cyanobacterial Gene Encoding a Membrane Protein Which Accumulates Under Iron Stress." In Progress in Photosynthesis Research, 773–76. Dordrecht: Springer Netherlands, 1987. http://dx.doi.org/10.1007/978-94-017-0519-6_161.

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Freibert, Sven-Andreas, Benjamin D. Weiler, Eckhard Bill, Antonio J. Pierik, Ulrich Mühlenhoff, and Roland Lill. "Biochemical Reconstitution and Spectroscopic Analysis of Iron–Sulfur Proteins." In Methods in Enzymology, 197–226. Elsevier, 2018. http://dx.doi.org/10.1016/bs.mie.2017.11.034.

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G. Ríos-Valencia, Diana, José Navarrete-Perea, Arturo Calderón-Gallegos, Jeannette Flores-Bautista, and Juan Pedro Laclette. "To Be or Not to Be a Tapeworm Parasite: That Is the Post-Genomic Question in Taenia solium Cysticercosis." In Current State of the Art in Cysticercosis and Neurocysticercosis [Working Title]. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.97306.

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Cestode parasites rely on their host to obtain their nutrients. Elucidation of tapeworm genomes has shown a remarkable reduction in the coding of multiple enzymes, particularly those of anabolic pathways. Previous findings showed that 10–13% of the proteins found in the vesicular fluid of Taenia solium cysticerci are of host origin. Further proteomic characterization allowed identification of 4,259 different proteins including 891 of host origin in the parasite’s protein lysates. One explanation for this high abundance and diversity of host proteins in the parasite lysates is related to the functional exploitation of host proteins by cysticerci. Supporting this concept is the uptake of host haptoglobin and hemoglobin by the parasite, as a way to acquire iron. Surprisingly, internalized host proteins are minimally degraded by the parasite physiological machinery. Additional proteomic analysis demonstrated that these host proteins become part of the organic matrix of calcareous corpuscles; as 60–70% of the protein content are host proteins. In this review, a collection of available genomic and proteomic data for taeniid cestodes is assembled, the subject of the use and processing of host proteins is particularly addressed; a sketchy and unique cell physiological profile starts to emerge for these parasitic organisms.
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Meurig Thomas, John. "Perutz and Kendrew: The Heroic Era of Structural Molecular Biology." In Architects of Structural Biology, 90–109. Oxford University Press, 2020. http://dx.doi.org/10.1093/oso/9780198854500.003.0005.

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When Perutz and Kendrew embarked on their determination of the structures of haemoglobin and myoglobin, most scientists felt that they would never succeed. These molecules contain approximately thousands of non-hydrogen atoms, whereas those molecules that had yielded to X-ray analysis previously contained fewer than a hundred non-hydrogen atoms. For real progress to be made in solving the structures of the giant proteins, a fundamentally new approach had to be evolved, which inter alia required massive computer power to handle the data contained in hundreds of thousands of X-ray diffraction patterns, and new experimental equipment like ultra-stable X-ray sources were required to record the diffraction data. The first successes were registered by Kendrew, who was able to reveal, in unprecedented detail, the atomically resolved structure of myoglobin with its haem group (containing a central iron atom) and all the details of the amino acid residues that constituted the backbone chain of the protein. Likewise, haemoglobin revealed its secrets. This also led to the discovery of sickle-cell anaemia, the first ever recorded molecular disease. It also shed new light on the pathology of anomalous haemoglobins in human populations.
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Marshall, Patricia, and Dora Marinova. "Health Benefits of Eating More Plant Foods and Less Meat." In Environmental, Health, and Business Opportunities in the New Meat Alternatives Market, 38–61. IGI Global, 2019. http://dx.doi.org/10.4018/978-1-5225-7350-0.ch003.

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The health benefits of eating more plant-based foods and less meat are scientifically proven. This chapter examines the evidence in relation to common health and medical conditions, such as cardiovascular diseases, type 2 diabetes, cancers, mental health, and dementia. It also analyzes the issues related to gastrointestinal health and diet in light of the presence of fiber and other plant materials. Although the environmental benefits of a plant-based diet are well-established, there are some concerns about the ability of such food choices to supply essential nutrients to the human body, such as protein, iron, vitamin B12, and Omega 3 fatty acids. They are discussed within the framework of a healthy diet. Some of the disadvantages of diets rich on animal proteins, such as heme iron, are highlighted with a warning that the consumption of lab-grown meat may carry similar risks. A balanced plant-rich diet seems a better and easier choice.
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Stehling, Oliver, Viktoria D. Paul, Janina Bergmann, Somsuvro Basu, and Roland Lill. "Biochemical Analyses of Human Iron–Sulfur Protein Biogenesis and of Related Diseases." In Methods in Enzymology, 227–63. Elsevier, 2018. http://dx.doi.org/10.1016/bs.mie.2017.11.004.

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Alsharekh, Alanoud. "Youth, Protest, and the New Elite." In The Changing Security Dynamics of the Persian Gulf, 165–90. Oxford University Press, 2018. http://dx.doi.org/10.1093/oso/9780190877385.003.0010.

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This chapter provides a critical analysis of the youth-led protests that shook Kuwaiti politics in 2011 and 2012 and threatened for a time to flare out of control. Alanoud Alsharekh analyzes the multiple roots of youth dissatisfaction with the political and economic status quo in Kuwait and explores the intersection of youth-led demands for change with the broader pressure points that led Kuwait from one political crisis to another after 2006. Alsharekh documents how both the Kuwaiti government and the established political opposition failed to capitalize on the emergence of the politically-active new youth movement. The rise of youth-led groups that break the mold of established political systems has implications for all other GCC states and Iran. Alsharekh’s concluding observations on the difficulties in assimilating the region’s youthful population into existing power-sharing mechanisms – as well as labor market structures – holds great comparative significance for future stability and sustainable growth.
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Potts, Charlotte R. "Conclusions." In Religious Architecture in Latium and Etruria, c. 900-500 BC. Oxford University Press, 2015. http://dx.doi.org/10.1093/oso/9780198722076.003.0016.

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This book began by stating that histories of religious architecture can be accounts of both buildings and people. This particular history, focused on the archaeological evidence for the development of cult buildings in early central Italy, has reconsidered traditional narratives about the form and function of Etrusco-Italic religious architecture and proposed an alternative reconstruction of how their architects and audiences may have interacted with one another in Rome, Latium, and Etruria between the ninth and the sixth centuries BC. Comparison with the construction of monumental temples elsewhere also indicated that settlements including Rome, Satricum, Pyrgi, and Tarquinia can perhaps be considered part of a network of Archaic Mediterranean settlements with material, commercial, and religious connections, and that monumental architecture may have been a mechanism for successful social interaction. This study has therefore supported the suggestion that the physical and social fabric of ancient communities were closely linked, and that regional studies of Latium and Etruria may furthermore benefit from being set in Italic and Mediterranean contexts. This concluding chapter briefly recapitulates the arguments made in the main body of the book and the significance of each of those arguments for studies of ancient architecture and society. It also assesses how these findings relate to broader debates about Archaic Italy. Finally, it acknowledges the limitations of this analysis and highlights opportunities for future research. Part I of this book demonstrated that ancient religious architecture was a protean phenomenon. Three chapters analysed the ambiguous evidence for Iron Age sacred huts, the range of different buildings types associated with ritual activities in the seventh century BC, and the emergence of a separate architectural language for religious buildings during the Archaic period. Detailed analyses of foundations and roofs revealed that as changes in technology and society led to the widespread use of more permanent building materials, the physical fabric of central Italic settlements was also increasingly marked by the use of particular architectural forms and decorations to differentiate cult buildings from other structures, setting them apart in a form of architectural consecration.
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Veguilla, Victoria. "Government and power relations." In Political Change in the Middle East and North Africa. Edinburgh University Press, 2017. http://dx.doi.org/10.3366/edinburgh/9781474415286.003.0007.

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This chapter analyses the change (or continuity) of MENA regimes in a post-Arab Spring context, focusing on governments and power relationships. This chapter firstly analyses the place governments occupy in their respective political systems; how they are perceived by their populations; and the extent to which are they capable of managing violence and imposing their authority across the whole of their national territory. Governments are responsible for the policies carried out in their countries. Thus, many of the social protests - predominantly focused on the high levels of corruption - were directed against governments. However, while governments are perceived to be the institutions responsible for meeting citizens’ welfare needs, there are other non-elected institutions (formal or informal) with significant decision-making powers that are non-accountable, such as the presidents of the republic, the monarchs, and other national (the armed forces in the case of Egypt; armed groups in the cases of Libya, Syria and Yemen) or international actors (such as Saudi Arabia and Iran). On the other hand, this chapter studies changes in the power structure. The author finds evidence of greater power concentration, with the exception of the new democratic regime of Tunisia.
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Conference papers on the topic "Iron proteins – Analysis"

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Islam, Nazmul, Davood Askari, and Tarek Trad. "Biocompatible Nanocomposite for Lab-on-a-Chip Application." In ASME 2011 International Mechanical Engineering Congress and Exposition. ASMEDC, 2011. http://dx.doi.org/10.1115/imece2011-64119.

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Lab-on-a-chip (LOC) devices integrate multiple laboratory functions and processes to a miniaturized chip format. Many LOC devices are used in a wide range of biomedical and other analytical applications including rapid pathogen detection, clinical diagnosis, electrophoresis, flow cytometry, and protein and DNA analysis. LOC devices can be fabricated from many types of material including various polymers, glass/silicon, or combinations of these materials. A broad variety of fabrication technologies are used for LOC device fabrication. LOC systems have several common features including microfluidics (e.g. channels, micro-pumps, mixers and valves) and sensing capabilities. This paper describes a technique for the fabrication of a micro-pump that can be used in implantable biocompatible devices. This paper will also discuss the synthesis and properties of biocompatible iron oxide nanoparticles (NPs) for AC electrokinetic micro-pumping. Iron oxide NP will be incorporated with PDMS (polydimithylsiloxane) to obtain biocompatible nanocomposite. The use of photoluminescence, hydrophobic, and reflective optical response of these materials for in-vitro and in-vivo sensing and micro-pumping will be highlighted.
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Yang, Bo, He-xi Wu, and Yi-bao Liu. "Simulation and Analysis: The Dose Distribution of KBS-3 Spent Nuclear Fuel Canister by MCNP." In 18th International Conference on Nuclear Engineering. ASMEDC, 2010. http://dx.doi.org/10.1115/icone18-29058.

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With the sustained and rapid development of the nuclear power plants, the spent fuel which is produced by the nuclear power plants will be rapidly rising. Spent fuel is High-level radioactive waste and should be disposed safely, which is important for the environment of land, public safety and health of the nuclear industry, the major issues of sustainable development and it is also necessary part for the nuclear industry activities. It is important to study and resolve the high-level radioactive waste repository problem. Spent nuclear fuel is an important component in the radioactive waste, The KBS-3 canister for geological disposal of spent nuclear fuel in Sweden consists of a ductile cast iron insert and a copper shielding. The ductile cast iron insert provides the mechanical strength whereas the copper protects the canister from corrosion. The canister inserts material were referred to as I24, I25 and I26, Spent nuclear fuel make the repository in high radiant intensity. The radiation analysis of canister insert is important in canister transport, the dose analysis of repository and groundwater radiolysis. Groundwater radiolysis, which produces oxidants (H2O2 and O2), will break the deep repository for spent nuclear fuel. The dose distribution of canister surface with different kinds of canister inserts (I24, I25 and I26) is calculated by MCNP (Ref. 1). Analysing the calculation results, we offer a reference for selecting canister inserts material.
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Sugiura, Hirotaka, Toshihisa Osaki, Hisatoshi Mimura, Tetsuya Yamada, and Shoji Takeuchi. "Dielecrophoretic introduction of the membrane proteins into the BLM platforms for the electrophygiological analysis systems." In 2020 IEEE/RSJ International Conference on Intelligent Robots and Systems (IROS). IEEE, 2020. http://dx.doi.org/10.1109/iros45743.2020.9341046.

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Yamaki, Daisuke, and Masahiko Hada. "Quantum-chemical analysis of paramagnetic [sup 13]C NMR shifts of iron-bound cyanide ions in heme-protein environments." In INTERNATIONAL CONFERENCE OF COMPUTATIONAL METHODS IN SCIENCES AND ENGINEERING 2009: (ICCMSE 2009). AIP, 2012. http://dx.doi.org/10.1063/1.4771843.

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