Academic literature on the topic 'Size exclusion chromatography (SEC)'

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Journal articles on the topic "Size exclusion chromatography (SEC)"

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Bajpai, Vivek K., Irfan A. Rather, and Alshammari Fanar Hamad. "Purification of bacteriocins using size-exclusion chromatography." Bangladesh Journal of Pharmacology 11, no. 2 (March 13, 2016): 281. http://dx.doi.org/10.3329/bjp.v11i2.25862.

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<p>The bacteriocin purification involves following main steps. a). Extraction of cell-free-supernatant of bacteria. b). Ammonium sulfate precipitation. c). Dialysis. d). Diafiltration using PVP and e). Size-exclusion chromatography. However, depending on the nature of work, the compound could be further analyzed by reverse-phase HPLC, NMR, mass spectrometry and sequencing.</p><p><strong>Video Clips</strong></p><p><a href="https://youtube.com/v/u1BmWfOTS9w">Part 1</a>: 4 min 52 sec</p><p><a href="https://youtube.com/v/aF45JFnwErc">Part 2</a>: 1 min 47 sec</p>
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YAMAGUCHI, Masato, Taro IIZUMI, Tetsuro YAMAMOTO, and Yoshiaki MOTOZATO. "Size-Exclusion Chromatography (SEC) of High Molecular Weight DNAs." NIPPON KAGAKU KAISHI, no. 7 (1993): 837–44. http://dx.doi.org/10.1246/nikkashi.1993.837.

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Pigeon, Michael G., and Alfred Rudin. "Correction for interdetector volume in size exclusion chromatography (SEC)." Journal of Applied Polymer Science 57, no. 3 (July 18, 1995): 287–301. http://dx.doi.org/10.1002/app.1995.070570305.

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Gaborieau, Marianne, and Patrice Castignolles. "Size-exclusion chromatography (SEC) of branched polymers and polysaccharides." Analytical and Bioanalytical Chemistry 399, no. 4 (October 22, 2010): 1413–23. http://dx.doi.org/10.1007/s00216-010-4221-7.

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Philip, C. V., and R. G. Anthony. "Separation of Coal Liquids by Size Exclusion Chromatography/Gas Chromatography (SEC/GC)." Journal of Chromatographic Science 24, no. 10 (October 1, 1986): 438–43. http://dx.doi.org/10.1093/chromsci/24.10.438.

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Badasyan, Artem, Andraž Mavrič, Irena Kralj Cigić, Tim Bencik, and Matjaz Valant. "Polymer nanoparticle sizes from dynamic light scattering and size exclusion chromatography: the case study of polysilanes." Soft Matter 14, no. 23 (2018): 4735–40. http://dx.doi.org/10.1039/c8sm00780b.

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Dynamic light scattering (DLS) and size exclusion chromatography (SEC), that are among the most popular methods for determining polymer nanoparticle (PNP) sizes, essentially depend on the quality of solution.
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Brandt, Josef, Johannes Lenz, Kai Pahnke, Friedrich Georg Schmidt, Christopher Barner-Kowollik, and Albena Lederer. "Investigation of thermoreversible polymer networks by temperature dependent size exclusion chromatography." Polymer Chemistry 8, no. 43 (2017): 6598–605. http://dx.doi.org/10.1039/c7py01262d.

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Jordan, Ashley, Mark Jacques, Catherine Merrick, Juliette Devos, V. Trevor Forsyth, Lionel Porcar, and Anne Martel. "SEC-SANS: size exclusion chromatography combinedin situwith small-angle neutron scattering." Journal of Applied Crystallography 49, no. 6 (November 2, 2016): 2015–20. http://dx.doi.org/10.1107/s1600576716016514.

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The first implementation and use of anin situsize exclusion chromatography (SEC) system on a small-angle neutron scattering instrument (SANS) is described. The possibility of deploying such a system for biological solution scattering at the Institut Laue–Langevin (ILL) has arisen from the fact that current day SANS instruments at ILL now allow datasets to be acquired using small sample volumes with exposure times that are often shorter than a minute. This capability is of particular importance for the study of unstable biological macromolecules where aggregation or denaturation issues are a major problem. The first use of SEC-SANS on ILL's instrument D22 is described for a variety of proteins including one particularly aggregation-prone system.
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Vianna-Soares, Cristina Duarte, Kim Cherng-Ju, and Michael Robert Borenstein. "HEMA/MMA/EDMA packing material evaluation for size exclusion chromatography (SEC)." Materials Research 8, no. 1 (March 2005): 15–21. http://dx.doi.org/10.1590/s1516-14392005000100005.

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Sidhom, Karim, Patience O. Obi, and Ayesha Saleem. "A Review of Exosomal Isolation Methods: Is Size Exclusion Chromatography the Best Option?" International Journal of Molecular Sciences 21, no. 18 (September 4, 2020): 6466. http://dx.doi.org/10.3390/ijms21186466.

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Extracellular vesicles (EVs) are membranous vesicles secreted by both prokaryotic and eukaryotic cells and play a vital role in intercellular communication. EVs are classified into several subtypes based on their origin, physical characteristics, and biomolecular makeup. Exosomes, a subtype of EVs, are released by the fusion of multivesicular bodies (MVB) with the plasma membrane of the cell. Several methods have been described in literature to isolate exosomes from biofluids including blood, urine, milk, and cell culture media, among others. While differential ultracentrifugation (dUC) has been widely used to isolate exosomes, other techniques including ultrafiltration, precipitating agents such as poly-ethylene glycol (PEG), immunoaffinity capture, microfluidics, and size-exclusion chromatography (SEC) have emerged as credible alternatives with pros and cons associated with each. In this review, we provide a summary of commonly used exosomal isolation techniques with a focus on SEC as an ideal methodology. We evaluate the efficacy of SEC to isolate exosomes from an array of biological fluids, with a particular focus on its application to adipose tissue-derived exosomes. We argue that exosomes isolated via SEC are relatively pure and functional, and that this methodology is reproducible, scalable, inexpensive, and does not require specialized equipment or user expertise. However, it must be noted that while SEC is a good candidate method to isolate exosomes, direct comparative studies are required to support this conclusion.
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Dissertations / Theses on the topic "Size exclusion chromatography (SEC)"

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Haider, Syed. "Enhanced gel electrophoresis (GE) and inductively coupled plasma-mass spectrometry (ICP-MS) based methods for the identification and separation of proteins and peptides." Thesis, Loughborough University, 2012. https://dspace.lboro.ac.uk/2134/10279.

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The main focus of the PhD study was to develop new gel electrophoresis and ICP-MS based methods to analyze a wide variety of the bio-molecules such as proteins, phosphoproteins and metalloproteins etc. The tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis (tricine-SDS-PAGE) method is commonly used to resolve low molecular mass proteins, however, it requires a high percentage gel and a very complicated procedure to achieve this separation. This study describes a modification to tricine-SDS-PAGE to make it more effective for the separation of smaller proteins and for coupling to ICP-MS. The modified method employs low percentage PAGE gels and low reagent concentrations that provide efficient separations, good quantitation and low matrix levels that are compatible with ICP-MS. This modified method was applied to analyze phosphopeptides. Phosphopeptides are very small in size and difficult to separate using the other techniques such as Laemmli SDS-PAGE, original tricine-SDS-PAGE, immobilized metal affinity chromatography (IMAC), size exclusion chromatography (SEC) etc. In this study a simplified procedure is described based on modifying the original tricine-SDS-PAGE method. A comparative study showed that this modified method successfully resolved a digest mixture of very low to high molecular mass phosphopeptides/peptides. In off-line coupling of this method with ICP-MS, much better recoveries of the peptides from the gel were obtained as compared to traditional methods which indicate the compatibility of this modified method for quantitative studies. An on-line coupling of the modified system with ICP-MS was also demonstrated and it was applied for the separation, detection and quantification of phosphopeptides. Another application of this modified system was the separation of serum proteins. Blood serum contains five major protein groups i.e., albumin, alpha-1 globulin, alpha-2 globulin, beta globulin and gamma globulin. The separation of these five major proteins in a single gel is difficult to achieve using traditional methods. The modified system was shown to be superior for the separation of these serum proteins in a 7% (m/v) native-PAGE gel and a cellulose acetate membrane. A further study was carried out into controlling the factors that cause metal loss and protein fragmentation in SDS-PAGE. Using a reducing sample buffer, and heating to high temperatures (90-100ºC) in alkaline or acidic conditions may cause protein fragmentation and decrease the metal binding affinity. 70ºC was found suitable to prepare the sample at neutral, alkaline or acidic pH as no fragmentation observed. To prevent metal loss, the binding constant (log K) values of metal-amino acids, play the major role. Those metals which have high binding affinities with the amino acids in proteins can also be affected by the variation of the pH so prior information about pH to maintain the binding constant values is essential to minimize metal loss. This was observed in the loss of zinc, and to a lesser extent copper from human serum albumin (HSA) as measured by inductively coupled plasma mass spectrometry (ICP-MS). The method described above was applied for the separation and quantification of the serum proteins obtained from age-related macular degeneration (AMD) patients (where the AMD patients were from Moorfields Eye Hospital, London). Zn and Cu were quantified employing external calibration. Zn concentration showed variation whilst Cu did not show any significant variations in samples from AMD patients. A brief study of the interaction of cisplatin and oxaliplatin with HSA and transferrin was also performed. Cisplatin bound much faster than oxaliplatin with HSA. After 24 hours incubation, cisplatin showed a decrease in signal intensity which indicates that cisplatin binding decreases with time. Cisplatin binding with transferrin as compared to HSA was not significant, which could be the result of unstable Pt-transferrin complex formation. Oxaliplatin did not show high binding to either protein, perhaps due to the presence of the bulky, non polar DACH ligand.
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Ghislain, Thierry. "Nature, origine et réactivité de la matière organique fossile dans les sols et sédiments : développements et applications de la photoionisation - spectrométrie de masse haute résolution (APPI-QTOF) et couplage avec la chromatograhie d'exclusion stérique (SEC)." Thesis, Nancy 1, 2011. http://www.theses.fr/2011NAN10070/document.

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Le développement des outils analytiques pour l'analyse de la matière organique complexe en géochimie organique a connu de nombreuses avancées ces dernières années. Ce développement a permis de répondre à un grand nombre de questions quant à la composition de la matière organique. Cependant, beaucoup des points restent encore à élucider comme notamment la caractérisation des fractions de hauts poids moléculaires ainsi que le suivi de la réactivité de la matière organique. Ce travail de thèse a eu pour objectif (i) d'adapter les techniques de spectrométrie de masse déjà existantes pour l'analyse de la matière organique fossile (notamment par la sélection de la source d'ionisation atmosphérique la plus adaptée) mais également (ii) de développer un nouveau type de couplage entre la chromatographie d'exclusion stérique (SEC) et la spectrométrie de masse APPI-QTOF pour l'analyse des fractions peu polaires de hauts poids moléculaires. L'adaptation du l'APPI-QTOF a tout d'abord permis de mieux comprendre la réactivité de contaminants organiques polyaromatiques en présence de phases minérales. Le couplage SEC-APPI-QTOF a, quant à lui, permis d'améliorer les connaissances sur la structure des asphaltènes. Cependant, malgré la « simplification » rendue possible par la SEC, la très grande quantité d'informations reste difficile à interpréter et prend beaucoup de temps. Un modèle mathématique a donc été développé basé sur des analyses numériques et statistiques des spectres de masse, permettant de les comparer entre eux afin de distinguer l'origine des échantillons et de suivre l'impact de processus physico-chimiques (altérations naturelles - traitements de remédiation)
The development of analytical tools for organic geochemistry analysis has increased these past years. This development has allowed answering many questions about organic matter composition. However, many issues remain to be clarified including the characterization of high molecular weight fractions and monitoring the reactivity of organic matter. This thesis has focused on both (i) existing method improvements for fossil organic geochemistry analysis but also on (ii) developing a new type of coupling between the size exclusion chromatography (SEC) and the APPI-QTOF mass spectrometry for high molecular weight weakly polar fractions. Adjustments on APPI-QTOF mass spectrometry have allowed a better understanding of polyaromatic organic contaminant reactivity in presence of mineral matrices. The success of this coupling has allowed a better understanding of the structure of asphaltenes. However despite the "simplification" obtained by the SEC, the large amount of information remains difficult to interpret and time-consuming. A mathematical model has been developed based on numerical and statistical analysis of mass spectra, allowing direct comparison of mass spectra and being able to identify several types of information such as origins of samples, monitoring of physico-chemical processes and also the efficiency of soil recovery treatments as well as the identification of analytical protocols
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Kapadi, Ajith Nayak. "Size Exclusion PEGylation Reaction Chromatography Modelling." The University of Waikato, 2006. http://hdl.handle.net/10289/2504.

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Size exclusion PEGylation reaction chromatography was investigated using a model developed by Fee (2005). Column dispersion was neglected and the PEGylation reaction was modelled as second order. The model allowed up to four PEG groups to be attached to a protein and accounted for succinic acid hydrolysis from activated PEG. The model was adapted to simulate a-lactalbumin PEGylation and succinic acid hydrolysis from activated PEG in a batch stirred tank so rate parameters from stirred tank kinetic experiments could be obtained and the model verified. The model was solved using finite differences and simulations run in Matlab. The effect of reaction parameters such as timing, length and concentration of PEG and protein injection, reaction rates, and model resolution on model simulation results was explored. In the size exclusion PEGylation simulations it was found that increasing protein concentration increased MonoPEG concentrations and increased the ratio of MonoPEG to starting protein feed concentration. Increasing PEG pulse length and starting PEG concentration initially increased MonoPEG concentration and product ratio until all protein had been PEGylated at which point MonoPEG concentration the product ratio levelled out. Increasing PEG hydrolysis rates did not affect the amount of MonoPEG produced but reduced the activated PEG concentration and increased succinic acid concentration. Optimal conditions for producing MonoPEG were found to be equal concentrations of PEG and protein, with the PEG injection length twice as long as the protein injection, and the PEG injection done immediately after the protein injection.
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Batas, Borislav. "Protein refolding using size exclusion chromatography." Thesis, University of Bath, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.337817.

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Popovici, Simona-Tereza. "Towards small and fast size-exclusion chromatography." [S.l. : Amsterdam : s.n.] ; Universiteit van Amsterdam [Host], 2004. http://dare.uva.nl/document/77409.

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Ziebell, Angela Louise. "Modelling lignin depolymerisation using size exclusion chromatography." Swinburne Research Bank, 2008. http://hdl.handle.net/1959.3/35984.

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Thesis (PhD) - Faculty of Life and Social Sciences, Swinburne University of Technology, 2008.
Presented for full assessment for the degree of Doctor of Philosophy, Faculty of Life and Social Sciences, Swinburne University of Technology - 2008. Typescript. Bibliography: p. 222-246.
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Torabi, Keivan. "Fourier transform infrared spectroscopy in size exclusion chromatography." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape7/PQDD_0002/MQ45901.pdf.

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Bayram-Hahn, Zöfre [Verfasser]. "Inverse size exclusion chromatography (ISEC) / Zöfre Bayram-Hahn." Mainz : Universitätsbibliothek der Johannes Gutenberg-Universität Mainz, 2007. http://d-nb.info/1230355758/34.

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Soponkanaporn, Teerapon. "Characterization by size exclusion chromatography of cationic polyelectrolyte degradation." Thesis, McGill University, 1988. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=74058.

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Rao, Baihua. "Size exclusion chromatography of polyolefins and evaluating local polydispersity." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1998. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp01/MQ33961.pdf.

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Books on the topic "Size exclusion chromatography (SEC)"

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Sadao, Mori. Size exclusion chromatography. Berlin: Springer, 1999.

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Mori, Sadao, and Howard G. Barth. Size Exclusion Chromatography. Berlin, Heidelberg: Springer Berlin Heidelberg, 1999. http://dx.doi.org/10.1007/978-3-662-03910-6.

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Hunt, B. J., and S. R. Holding, eds. Size Exclusion Chromatography. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4615-7861-1.

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Potschka, Martin, and Paul L. Dubin, eds. Strategies in Size Exclusion Chromatography. Washington, DC: American Chemical Society, 1996. http://dx.doi.org/10.1021/bk-1996-0635.

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Striegel, Andre M., ed. Multiple Detection in Size-Exclusion Chromatography. Washington, DC: American Chemical Society, 2004. http://dx.doi.org/10.1021/bk-2005-0893.

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1967-, Striegel André M., American Chemical Society. Division of Analytical Chemistry, American Chemical Society. Division of Polymer Chemistry, American Chemical Society. Division of Polymeric Materials: Science and Engineering, and American Chemical Society Meeting, eds. Multiple detection in size-exclusion chromatography. Washington, DC: American Chemical Society, 2004.

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Provder, Theodore, ed. Detection and Data Analysis in Size Exclusion Chromatography. Washington, DC: American Chemical Society, 1987. http://dx.doi.org/10.1021/bk-1987-0352.

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Torabi, Keivan. Fourier transform infrared spectroscopy in size exclusion chromatography. Ottawa: National Library of Canada, 1999.

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Rao, Baihua. Size exclusion chromatography of polyolefins and evaluating local polydispersity. Ottawa: National Library of Canada, 1998.

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Podzimek, Stepan. Light Scattering, Size Exclusion Chromatography and Asymmetric Flow Field Flow Fractionation. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2011. http://dx.doi.org/10.1002/9780470877975.

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Book chapters on the topic "Size exclusion chromatography (SEC)"

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Mori, Sadao, and Howard G. Barth. "SEC Method Development." In Size Exclusion Chromatography, 55–76. Berlin, Heidelberg: Springer Berlin Heidelberg, 1999. http://dx.doi.org/10.1007/978-3-662-03910-6_5.

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Schrag, Delphine, Marie Corbier, and Sylvain Raimondi. "Size Exclusion-High-Performance Liquid Chromatography (SEC-HPLC)." In Methods in Molecular Biology, 507–12. Totowa, NJ: Humana Press, 2014. http://dx.doi.org/10.1007/978-1-62703-992-5_31.

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Reshi, Qurat Ul Ain, Mohammad Mehedi Hasan, Keerthie Dissanayake, and Alireza Fazeli. "Isolation of Extracellular Vesicles (EVs) Using Benchtop Size Exclusion Chromatography (SEC) Columns." In Methods in Molecular Biology, 201–6. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1246-0_14.

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Fossati, Andrea, Fabian Frommelt, Federico Uliana, Claudia Martelli, Matej Vizovisek, Ludovic Gillet, Ben Collins, Matthias Gstaiger, and Ruedi Aebersold. "System-Wide Profiling of Protein Complexes Via Size Exclusion Chromatography– (SEC–MS)." In Shotgun Proteomics, 269–94. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1178-4_18.

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Guadalupe, Zenaida, Belén Ayestarán, Pascale Williams, and Thierry Doco. "Determination of Must and Wine Polysaccharides by Gas Chromatography–Mass Spectrometry (GC–MS) and Size-Exclusion Chromatography (SEC)." In Polysaccharides, 1–28. Cham: Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-03751-6_56-1.

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Guadalupe, Zenaida, Belén Ayestarán, Pascale Williams, and Thierry Doco. "Determination of Must and Wine Polysaccharides by Gas Chromatography-Mass Spectrometry (GC-MS) and Size-Exclusion Chromatography (SEC)." In Polysaccharides, 1–28. Cham: Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-03751-6_56-2.

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Guadalupe, Zenaida, Belén Ayestarán, Pascale Williams, and Thierry Doco. "Determination of Must and Wine Polysaccharides by Gas Chromatography-Mass Spectrometry (GC-MS) and Size-Exclusion Chromatography (SEC)." In Polysaccharides, 1265–97. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-16298-0_56.

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Montaudo, Maurizio S. "Size-Exclusion Chromatography/Matrix-Assisted Laser Desorption Ionization and SEC/NMR Techniques for Polymer Characterization." In ACS Symposium Series, 152–67. Washington, DC: American Chemical Society, 2004. http://dx.doi.org/10.1021/bk-2005-0893.ch009.

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Thomsen, Maren. "Determination of the of Membrane Using Size-Exclusion Chromatography with Multiangle Laser Light Scattering (SEC-MALLS)." In Methods in Molecular Biology, 263–69. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0724-4_12.

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Cutler, Paul. "Size-Exclusion Chromatography." In Springer Protocols Handbooks, 719–29. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-60327-375-6_41.

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Conference papers on the topic "Size exclusion chromatography (SEC)"

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Strachan, S., E. Kontopoulou, D. Reinhardt, B. Giebel, and B. Thakur. "Comparison of differential ultracentrifugation (DC) and size exclusion chromatography (SEC) based exosome isolation methods." In 31. Jahrestagung der Kind-Philipp-Stiftung für pädiatrisch onkologische Forschung. Georg Thieme Verlag KG, 2018. http://dx.doi.org/10.1055/s-0038-1645025.

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Stachowiak, Jeanne C., Erin E. Shugard, Pamela Caton, Bruce P. Mosier, Ron Renzi, Rafael V. Davalos, Gregory J. McGraw, Blake A. Simmons, Victoria A. Vandernoot, and Brent A. Haroldsen. "Automated Sample Preparation System for Rapid Biological Threat Detection." In ASME 2005 International Mechanical Engineering Congress and Exposition. ASMEDC, 2005. http://dx.doi.org/10.1115/imece2005-80945.

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Rapid, automated sample preparation of bacterial cells and spores is required for threat analysis by remotely deployed chemical and biological warning systems. Sandia is designing, building, and testing an automated front-end sample preparation system based on miniature and microfluidic components, with the goal of concentrating bacterial species collected from the air, harvesting and solubilizing proteins from them, and delivering them to Sandia’s MicroChemLab capillary gel electrophoresis system1,2 for analysis (Fig. 1). Miniature, motorized valves and pumps control flow between system components connected by fused silica capillaries (Fig. 4). Sample processing modules include concentration by dielectrophoresis in an array of insulating posts or by mechanical filtration; heat-activated chemical lysis; mechanical filtration; removal of chemical lysis agents by size exclusion chromatography (SEC); and in-capillary fluorescent labeling.
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Johnson, Geoffrey, Mehrdad Hesampour, Susanna Toivonen, Sirkku Hanski, Stina Sihvonen, Nancy Lugo, Jennifer McCallum, and Michael Pope. "Confirmation of Polymer Viscosity Retention at the Captain Field Through Wellhead Sampling." In SPE Improved Oil Recovery Conference. SPE, 2022. http://dx.doi.org/10.2118/209370-ms.

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Abstract The Ithaca-operated Captain field is located in Block 13/22a in the U.K. sector of the North Sea, 130 km northeast of Aberdeen, in a water depth of 360 ft. The Captain Field has an adverse mobility ratio across all the producing reservoirs and so has undergone improved oil recovery by polymer flooding since 2011 using Anionic polyacrylamide (HPAM) in liquid form. This paper presents recent offshore wellhead sampling from the Captain facility that confirms high polymer solution viscosity retention from a producing well, even after significant mechanical degradation through the Electrical Submersible Pumps (ESP), which is used for artificial lift. The continuing commercial success of the Captain Field polymer flood is underpinned by maintaining polymer viscosity throughout the system. High polymer returns, combined with declining oil rates, may result in the continued operation of these wells to be unattractive. This paper summarises the data used to shut-in mature wells that are producing polymer to the surface, to enable the polymer flood to continue displacing oil to offset production wells. Samples were collected from the wellhead in oxygen free conditions into pressurized cylinders. The measurements in laboratory were taken inside a glove box to avoid oxygen ingress. The absence of oxygen was confirmed through measurements of dissolved oxygen and redox potential. Viscosity of the solutions have been measured with Brookfield viscometer inside the glove box and the results were compared to the expected viscosity from fresh non-degraded polymer solution. The expected viscosity was determined using a concentration – viscosity curve of a fresh polymer in synthetic Captain brine. Polymer solution concentration is measured on-site using KemConnect™ EOR, a time resolved fluorescence method, the collected samples were subsequently confirmed with size exclusion chromatography (SEC) in the laboratory. The polymer concentrations measured from these wellhead samples with KemConnect™ EOR were in the region of 700-900 ppm. Previously collected downhole viscosity samples confirmed &gt;70% viscosity retention prior to being produced through the ESP, while 50-80% of the original viscosity was found to be retained after production through the ESP to the surface facilities under anaerobic conditions for the range of concentrations sampled. These findings demonstrate the resilience of the polymer product to degradation in a real-world operational setting. It also provides data that may be used to estimate the expected downhole polymer solution viscosity from wellhead samples for defined operating conditions. The ability to estimate polymer solution downhole viscosity retention from wellhead samples provides a simpler and less expensive method of estimating viscosity retention than downhole sampling, which is especially useful for wells that do not have downhole access for sample collection.
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Muller, A. J., and R. L. Opila. "A new rapid screening method for silicones by size exclusion chromatography." In Electrical Contacts, 1988., Proceedings of the Thirty Fourth Meeting of the IEEE Holm Conference on Electrical Contacts. IEEE, 1988. http://dx.doi.org/10.1109/holm.1988.16131.

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Handa, M., K. Titani, K. Takio, and Z. M. Ruggeri. "CHARACTERIZATION OF THE VON WILLEBRAND FACTOR-BINDING DOMAIN OF PLATELET MEMBRANE GLYCOPROTEIN Ib." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642925.

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We have previously obtained immunochemical evidence that the von Willebrand factor (vWF)-binding domain of the platelet membrane glycoprotein (GP) Ib is located near the amino terminus of the a subunit (Journal of Biological Chemistry 261: 12579-12585, 1986). We have now determined the complete amino acid sequence of the 45 kDa tryptic fragment of glycocalicin that contains this domain. Purified glycocalicin was subjected to limited digestion with trypsin and the proteolytic fragments were separated by size-exclusion high-pressure liquid chromatography. Two fragments of 45 kDa and 84 kDa, respectively, were obtained under nonreducing conditions. After reduction and S-carboxymethylation, the 84 kDa fragment was unchanged, while the 45 kDa fragment yielded two new fragments, one of 35 kDa and the other of 7 kDa. This finding proves the existence of a trypsin cleavage site within a disulfide loop. Two primary sets of overlapping fragments were obtained by cleavage of the carboxymethylated protein at methionyl and lysyl bonds following treatment with cyanogen bromide and Achromobacter protease I, respectively. Additional fragments were obtained by treatment of glycocalicin with Staphylococcus aureus V8 protease and Serratia marcescens protease. Analysis of all these fragments provided data that allowed determination of the sequence of the amino terminal 299 residues of the GP Ib a-chain. This includes the 45 kDa tryptic fragment containing the vWF-binding domain. This 299-residue sequence, corresponding approximately to two thirds of the α-chain polypeptide, is largely hydrophobic and contains only two N-linked and one O-linked carbohydrate chains. A hydrophilic region exists between residues 215-299, with a cluster of ten negatively charged residues at 269-287. This area is likely to attract positively charged molecules. The hydrophilic, highly glycosylated (at Ser/Thr residues) region corresponding to the previously described "macroglycopeptide" begins at residue 292. The determined sequence of glycocalicin contains a region with seven repeats, indicative of gene duplication, and is highly homologous to human leucine-rich α2-glycoprotein.
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Medeiros, Ingrid, Hilton Nascimento, Eduardo Gomes, Melissa Premazzi, Jaline Silvério, Erica Fonseca, and Daniel Guedes Jr. "Optimization of high performance liquid chromatography by size exclusion and reversed phase for homogeneity analysis of recombinant human erythropoietin." In I Seminário Anual Científico e Tecnológico em Imunobiológicos. Instituto de Tecnologia em Imunobiológicos, 2013. http://dx.doi.org/10.35259/isi.sact.2013_27331.

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Ray, Manas K., and Susan Guo. "CARBOHYDRATE STRUCTURAL CHARACTERIZATION OF RECOMBINANT HUMAN ICAM-1 DES454-532 PRODUCED IN CHINESE HAMSTER OVARY CELLS BY ANION-EXCHANGE CHROMATOGRAPHY, SIZE-EXCLUSION CHROMATOGRAPHY AND MALDI-TOF-MS." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.795.

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Carson, K. E., and C. R. Woolard. "Characterization of Natural Organic Material in Alaska Drinking Water Sources Using High Performance Size-Exclusion Chromatography with Ultraviolet Absorbance Detection." In World Water and Environmental Resources Congress 2005. Reston, VA: American Society of Civil Engineers, 2005. http://dx.doi.org/10.1061/40792(173)104.

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Dykas, Brian, Timothy Krantz, Gordon Berger, Kenneth W. Street, and Wilfredo Morales. "Grease Degradation in Critical Helicopter Drivetrain Bearings." In STLE/ASME 2010 International Joint Tribology Conference. ASMEDC, 2010. http://dx.doi.org/10.1115/ijtc2010-41200.

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An investigation of critical aviation bearings lubricated with MIL-PRF-81322 grease was conducted to derive an understanding of the mechanisms of grease degradation and the loss of lubrication over time. Chemical analysis was performed on grease samples from fielded bearings and compared to fresh grease and samples taken from bearings run for extended times in a laboratory environment. Size exclusion chromatography and Fourier transform infrared spectroscopy were used to investigate the condition of the grease, and evidence of additive depletion, oil evaporation, and thickener degradation were seen, consistent with results reported by other authors. Given the relatively light loading conditions experienced by the test bearings, they were able to continue operating at high temperature despite having most of the original oil depleted from the grease.
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Rodriguez, L., S. Antignard, B. Giovannetti, G. Dupuis, N. Gaillard, S. Jouenne, G. Bourdarot, D. Morel, A. Zaitoun, and B. Grassl. "A New Thermally Stable Synthetic Polymer for Harsh Conditions of Middle East Reservoirs: Part II. NMR and Size Exclusion Chromatography to Assess Chemical and Structural Changes During Thermal Stability Tests." In SPE Improved Oil Recovery Conference. Society of Petroleum Engineers, 2018. http://dx.doi.org/10.2118/190200-ms.

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Reports on the topic "Size exclusion chromatography (SEC)"

1

Mauritz, Kenneth A., and Robson F. Storey. Size Exclusion Chromatography System. Fort Belvoir, VA: Defense Technical Information Center, March 2001. http://dx.doi.org/10.21236/ada393948.

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Dickens, B., and F. L. McCrackin. System of hardware and software developed for size exclusion chromatography. Gaithersburg, MD: National Bureau of Standards, 1987. http://dx.doi.org/10.6028/nbs.ir.87-3669.

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Coulombe, S. Comparison of detectors for size exclusion chromatography of heavy oil related samples. Natural Resources Canada/ESS/Scientific and Technical Publishing Services, 1986. http://dx.doi.org/10.4095/302666.

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Márquez-Ruiz, Gloria. Analysis of Used Frying Oils and Fats by High-Performance Size-Exclusion Chromatography. AOCS, June 2011. http://dx.doi.org/10.21748/lipidlibrary.39204.

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Beyer, Frederick L., Eugene Napadensky, and Christopher R. Ziegler. Characterization of Polyamide 66 Obturator Materials by Differential Scanning Calorimetry and Size-Exclusion Chromatography. Fort Belvoir, VA: Defense Technical Information Center, December 2005. http://dx.doi.org/10.21236/ada444191.

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Rahimi, P. M., and J. F. Kelly. Size exclusion chromatography for characterization of heavy oil/bitumen vacuum bottoms as feedstocks for coprocessing. Natural Resources Canada/ESS/Scientific and Technical Publishing Services, 1986. http://dx.doi.org/10.4095/302664.

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Coulombe, S., and S. Desjardins. Investigation of new column packings for molecular weight determination of heavy fractions by size exclusion chromatography. Natural Resources Canada/ESS/Scientific and Technical Publishing Services, 1987. http://dx.doi.org/10.4095/304359.

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