Готові списки джерел за темами / Chromatographic purification

Добірка наукової літератури з теми "Chromatographic purification"

Автор: Grafiati
Опубліковано: 30 травня 2022
Оновлено: 31 травня 2022

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Статті в журналах з теми "Chromatographic purification"

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Hakala, Sari H., and I. Marina Heinonen. "Chromatographic Purification of Natural Lycopene." Journal of Agricultural and Food Chemistry 42, no. 6 (June 1994): 1314–16. http://dx.doi.org/10.1021/jf00042a012.

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2

Ngo, That T., Sherryline Jogie‐Brahim, and Dyer Narinesingh. "Affinity Chromatographic Purification of Antibodies." Analytical Letters 40, no. 15 (October 2007): 2799–820. http://dx.doi.org/10.1080/00032710701653111.

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3

Suetsuna, T., N. Dragoe, H. Shimotani, A. Takeda, S. Ito, R. J. Cross, M. Saunders, H. Takagi, and K. Kitazawa. "CHROMATOGRAPHIC PURIFICATION OF Kr@C60." Fullerenes, Nanotubes and Carbon Nanostructures 10, no. 1 (April 15, 2002): 15–21. http://dx.doi.org/10.1081/fst-120002926.

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4

Peterson, Robert E., Gail M. Shannon, and Odette L. Shotwell. "Purification of Cyclopiazonic Acid by Liquid Chromatography." Journal of AOAC INTERNATIONAL 72, no. 2 (March 1, 1989): 332–35. http://dx.doi.org/10.1093/jaoac/72.2.332.

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Abstract A purification procedure for cyclopiazonic acid has been developed, using sequential preparative and semi-preparative liquid chromatography. Crude cyclopiazonic acid (324 mg) was extracted from a 1 L fermentation medium with chloroform-methanol (80 + 20), dried, dissolved in chloroform, and chromatographed on an oxalic acid/ silica preparative column with chloroform-methanol (99 + 1) as the eluant. A semi-preparative oxalic acid/silica column and chloroform- methanol (99.5 + 0.5) were then used for rechromatography of the partially purified cyclopiazonic acid. This second chromatographic treatment yielded fractions from which cyclopiazonic acid was readily crystallized (106.7 mg; 33% recovery). Analytical chromatography was developed using an amino column in an ion-exchange mode, with a methanol-phosphate buffer eluant. Response was linear from 10 to 800 μg/injection of standard solutions. Cyclopiazonic acid chemically binds sodium from soda-lime vials.
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5

Wang, Zhiyong, Haruka Omachi, and Hisanori Shinohara. "Non-Chromatographic Purification of Endohedral Metallofullerenes." Molecules 22, no. 5 (April 29, 2017): 718. http://dx.doi.org/10.3390/molecules22050718.

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O'Riordan, C. "Chromatographic purification of adenovirus and AAV." Biofutur 1997, no. 167 (May 1997): 48. http://dx.doi.org/10.1016/s0294-3506(99)80367-6.

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Surovtsev, V. I., V. M. Borzenkov, and V. P. Levchuk. "Purification of bacteriocins by chromatographic methods." Applied Biochemistry and Microbiology 51, no. 9 (October 31, 2015): 881–86. http://dx.doi.org/10.1134/s0003683815090069.

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Brooks, C. A., S. M. Cramer, and T. G. Rosano. "Preparative chromatographic purification of cyclosporine metabolites." Clinical Chemistry 39, no. 3 (March 1, 1993): 457–66. http://dx.doi.org/10.1093/clinchem/39.3.457.

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Abstract Polar and primary metabolites of cyclosporin A (CsA) have successfully been isolated by a novel separation protocol. An efficient, easy-to-scale-up chromatographic adsorption/desorption operation recovers polar and primary CsA metabolite pools from large volumes of urine; purified CsA metabolites are subsequently obtained by high-resolution preparative elution chromatography of the semipurified metabolite pools. Separations performed on a semipreparative scale [with a 250 x 9.4 mm (i.d.) reversed-phase HPLC column] yielded microgram quantities of CsA metabolites at > 97% purity, as determined by fast atom bombardment mass spectrometry. These separations also yielded two previously unreported CsA metabolites, similar to AM1A but with an additional hydroxylation. The yield of metabolites was increased to several milligrams by performing the separations with a preparative-scale [250 x 21.2 mm (i.d.)] reversed-phase column. The production rate of purified primary CsA metabolites was greatly increased by performing the separation with the preparative-scale column under conditions of severe mass overloading. In a single chromatographic run, we successfully isolated 11.0 and 5.0 mg of AM1 and AM1c, respectively, at a purity of > 97%. As expected, this increase in the yield of purified metabolites was accompanied by a decrease in the overall recovery. This separation scheme enables the rapid processing of large volumes of urine for isolation of the milligram quantities of CsA metabolites necessary to assess their biological activity. The procedure is applicable to small- or large-scale metabolite isolation and provides a ready source of purified metabolites for in vitro and whole-animal studies.
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Adamíková, Jana, Monika Antošová, and Milan Polakovič. "Chromatographic purification of recombinant human erythropoietin." Biotechnology Letters 41, no. 4-5 (February 27, 2019): 483–93. http://dx.doi.org/10.1007/s10529-019-02656-8.

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Wood, David W. "Non-Chromatographic Recombinant Protein Purification by Self-Cleaving Purification Tags." Separation Science and Technology 45, no. 15 (October 4, 2010): 2245–57. http://dx.doi.org/10.1080/01496395.2010.507665.

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Дисертації з теми "Chromatographic purification"

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Hamdi, Anis. "Novel Chromatographic methodology for virus particles purification." Master's thesis, Universidade Nova de Lisboa, Instituto de Tecnologia Química e Biológica António Xavier, 2016. http://hdl.handle.net/10362/64186.

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"Virus based biopharmaceuticals are considered the most dynamic adopted tools in modern therapeutic medicine. Their use is increasing in the fields of vaccination and gene therapy. Membrane chromatography is becoming an attractive alternative t ool that can be used for virus purification due to its scalability, potential for optimization and economical features, allowing higher productivities with lower DSP costs. (…)"
N/A
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Mekaoui, Nazim. "Contribution à l'étude de la chromatographie à contre-courant : partage de composés ionisables, nouvelles colonnes et purification séquentielles." Thesis, Lyon 1, 2012. http://www.theses.fr/2012LYO10249/document.

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La chromatographie à contre courant (CCC) est une technique de purification chimique préparative quitravaille avec un système biphasique liquide. Une phase est la phase mobile, l'autre phase est la phasestationnaire. Il n'y a aucun support solide: un champ de force centrifuge est utilisé pour maintenir en place laphase stationnaire. Ce travail est une contribution à l'étude de la purification préparative par CCC. Après uneimportante étude bibliographique des procédés de purification en continu tant en CCC qu'autres, il est montréque la méthode dite "multi-dual-mode", ou MDM, est une solution possible. Elle consiste à utiliser le fait queles deux phases liquides peuvent servir de phase stationnaire: il suffit d'inverser le sens de circulation et lanature de la phase mobile (méthode dual-mode). Le mélange est séparé de façon classique pendant untemps chronométré, puis on inverse le rôle des phases: la phase mobile devient stationnaire et vice versa eton inverse également le sens de circulation (ascendant devient descendant ou vice versa). On sort lescomposants du mélange soit d'un coté de la colonne CCC, soit de l'autre. La méthode est mise en oeuvrepour purifier le Bleu de Coomassie en le débarassant des ses composés polaires (d'un coté) et apolaire (del'autre coté de la colonne et en accumulant dans la colonne la fraction de polarité intermédiaire, fractiond'intérêt. Une nouvelle colonne hydrostatique de petit volume (30 mL) a également été testée: elle permetde tester un nouveau système liquide très rapidement
Counter-current chromatography (CCC) is a preparative purification technique that works with the twoliquid phases of a biphasic liquid system. One phase is used as the mobile phase when the other phase isused as the stationary phase. There is no solid support: centrifugal fields are used to obtain a support-freeliquid stationary phase. This work contains an exhaustive bibliographic study of what can be found in theliterature concerning continuous chromatographic processes. The multi-dual-mode (MDM) process was foundto be the best one able to purify large amount of crude mixtures. The MDM method starts with a classicalseparation of the mixture followed by a switch of both the liquid phase nature and the flowing direction. Themobile phase flowing e.g. in a descending direction becomes the stationary phase. The previous stationaryphase becomes the mobile phase flowing in the ascending direction (or vice versa). The purified compoundsof the introduced mixture are eluted at one side of the column or the other according to their polarity. TheMDM method was used to purify a crude sample of Coomassie Blue: the polar part of the dye was eluted atthe column top (or head) and the apolar part at the column bottom (or tail) while the essential part of the dyewas trapped inside the CCC column. The work also presents a new small volume (30 mL) hydrostatic CCCcolumn. It is shown that this column could be used to test quickly the potential of a given biphasic liquidsystem
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Balci, Oguz. "Affinity chromatographic purification of recombinant human growth hormone." Master's thesis, METU, 2008. http://etd.lib.metu.edu.tr/upload/2/12609269/index.pdf.

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The purpose of the study is to purify human growth hormone from the fermentation broth by affinity chromatography. For this purpose, human growth hormone specific oligonucleotide aptamers are selected among an aptamer library
selected oligonucleotides were synthesized and used as ligands. Effect of pH on ligand-human growth hormone complex formation was investigated and the highest complex formation was obtained at pH= 7.0. Human growth hormone is separated from the fermentation broth with 99.8% purity and 41% overall yield. The equilibrium data obtained was described by Langmuir type isotherm where saturation constant (q0) and affinity constant (K) are calculated as 0.338 mg hGH/µ
mol aptamer and 0.059 mg hGH/ml, respectively. Further, equilibrium data obtained using aptamer affinity column was described by Langmuir type isotherm where saturation constant (q0) and affinity constant (K) are 0.027 mg hGH/µ
mol aptamer and 1.543 mg hGH/ml, respectively. It is possible that, selected aptamer can be used for purification of bulk amounts of recombinant human growth hormone by using aptamer affinity chromatography.
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Ramat, Fabien M. "Protein purification using expanded bed chromatography." Link to electronic thesis, 2003. http://www.wpi.edu/Pubs/ETD/Available/etd-0114104-114704.

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Thesis (M.S.)--Worcester Polytechnic Institute.
Keywords: zirconia; protein purification; anion exchange; chicken egg white; expanded bed chromatography. Includes bibliographical references (p. 83-86).
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Nakamura, Koji. "Studies on High-performance Affinity Chromatography : Preparation of the Chromatographic Gels, Evaluation of the Chromatographic Conditions, and the Application to Purification of Enzymes." Kyoto University, 2004. http://hdl.handle.net/2433/148344.

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Bergs, Dominik [Verfasser]. "A contribution to chromatographic purification of natural products / Dominik Bergs." München : Verlag Dr. Hut, 2013. http://d-nb.info/1045989150/34.

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Ramat, Fabien M. "Protein purification using expanded bed chromatography." Digital WPI, 2004. https://digitalcommons.wpi.edu/etd-theses/92.

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Expanded bed chromatography using ion-exchange media is a powerful first step in purification processes. Expanded bed chromatography can be used to extract components from complex and viscous solution. This can be achieved because of the void created between adsorbent particles where as in packed bed chromatography, the adsorbent is too compact and dense for a complex feed stock to flow through. Expanded bed chromatography was used to purify bovine serum albumin (BSA) from chicken egg white (CEW). The high viscosity of CEW presents a unique challenge for efficient large-scale protein purification. This project aimed to optimize and evaluate a separation method that is believed to be particularly suitable for high viscosity solutions: expanded-bed ion exchange chromatography. The BSA was admixed into the CEW and the solution was pumped through the column for purification. The media used in the column was Streamline DEAE which is an anion-exchanger. The yield obtained was 85% and the purity was 57%. A mathematical model to understand and predict the behavior of expanded bed chromatography was developed to provide an estimation of the breakthrough curves obtained for BSA. A small sized porous dense adsorbent was also synthesized to enhance the purification process. This zirconia-based adsorbent allows use of higher flow velocities that is a key factor when working with viscous fluids such as chicken egg white.
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Pate, Martin Eric. "A practical investigation into the use of principal component analysis for the modelling and scale-up of high performance liquid chromatography." Thesis, University College London (University of London), 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.322003.

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Kochendörfer, Kiara [Verfasser]. "Chromatographic Purification of an Intermediately Eluting Component from a Complex Mixture / Kiara Kochendörfer." München : Verlag Dr. Hut, 2017. http://d-nb.info/1126297976/34.

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Jin, J. "Lipid foulant interactions during the chromatographic purification of virus-like particles from Saccharomyces cerevisiae." Thesis, University College London (University of London), 2011. http://discovery.ucl.ac.uk/1302065/.

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The objective of this study was to understand the mechanism of lipid fouling in chromatography through the investigation of a hydrophobic interaction chromatography (HIC) operation. This was motivated by the need to understand this phenomenon during the manufacture of biological products such as vaccines. The systematic approach and novel analytical techniques employed create a unique platform to study fouling of other chromatographic adsorbents and process feed materials. HIC is employed as a primary capture step in the purification of yeast derived hepatitis R surface antigen (HBsAg), where the required cell disruption and detergent liberation steps release high levels of lipid content into the feed stream. From lipid- rich and lipid-depleted feedstocks, comparative analysis was able to quantify the deterioration in HIC performance (binding capacities, purities and recoveries) under successive cycles. Furthermore, a full mass balance on host lipids identified the highly hydrophobic triacylglyceride as the main foulant. Intra-particle distribution and progression of lipid fouling and its effects on material adsorption and diffusion were then examined under confocal laser scanning microscopy (CLSM). In addition, high- resolution scanning electron microscopy (SEM) images of the fouled bead (after 40 cycles) confirmed that a thick lipid layer was building up on the outer bead surface. Based on these findings, the mechanism of fouling was thought to be the rapid accumulation of lipid foulant at the rim of the bead, which was aggravated by the possible diffusion hindrance resulting from multi layer adsorption. Finally, pretreatments to reduce this mechanism of chromatography fouling were evaluated in terms of improvement on feed quality and HIC performance. Selective adsorbent polystyrene XAD-4 demonstrated promising lipid removal capabilities with satisfactory HBsAg VLP recoveries. The improved feed into the column resulted in a three-fold increase in product capacity, whilst the overall yield remained constant over 40 cycles.
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Книги з теми "Chromatographic purification"

1

International, Strategic Directions. Purification applications for liquid chromatography: Stellar growth beyond the laboratory. Los Angeles: Strategic Directions International, 2004.

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International, Strategic Directions. Purification chromatography: The key to the biopharmacuetical industry, 2011-2016. Los Angeles: Strategic Directions International, 2012.

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3

P, Hanna Christopher, and Hornby D, eds. DNA chromatography. Weinheim: Wiley-VCH, 2002.

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4

Gjerde, Douglas T. RNA purification and analysis: Sample preparation, extraction, chromatography. Weinheim: Wiley-VCH, 2009.

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5

Lan, Chi-Wei. Protein purification using fluidised bed chromatography: Physical and biochemical characterisation of a simple absorbent contactor. Birmingham: University of Birmingham, 2000.

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6

Meer, Andries Piet van der. On counter-current fluidized ion-exchange columns. [Delft?: S. n., 1985.

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7

Protein affinity tags: Methods and protocols. New York: Humana Press, 2014.

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(Editor), Jan-Christer Janson, and Lars Ryden (Editor), eds. Protein Purification. Wiley-VCH, 1989.

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9

Gottschalk, Uwe. Process Scale Purification of Antibodies. Wiley & Sons, Incorporated, John, 2009.

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Gottschalk, Uwe. Process Scale Purification of Antibodies. Wiley & Sons, Incorporated, John, 2011.

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Частини книг з теми "Chromatographic purification"

1

Stein, William H. "Chromatographic Purification of Ribonuclease and Lysozyme." In Novartis Foundation Symposia, 17–30. Chichester, UK: John Wiley & Sons, Ltd, 2008. http://dx.doi.org/10.1002/9780470718872.ch3.

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Vandevyver, Caroline, and Ruth Freitag. "Purification of Antibodies by Chromatographic Methods." In Antibodies, 133–68. Boston, MA: Springer US, 2004. http://dx.doi.org/10.1007/978-1-4419-8875-1_5.

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Lee, Jenny, Shalini Gupta, Jin-Sheng Huang, Lasanthi P. Jayathilaka, and Bao-Shiang Lee. "Preparation and Purification of Garlic-Derived Organosulfur Compound Allicin by Green Methodologies." In Green Chromatographic Techniques, 123–39. Dordrecht: Springer Netherlands, 2013. http://dx.doi.org/10.1007/978-94-007-7735-4_6.

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Datta, Sriparna, Runa Ghosh Auddy, and Amit De. "Supercritical Fluid Chromatography: A Green Approach for Separation and Purification of Organic and Inorganic Analytes." In Green Chromatographic Techniques, 55–80. Dordrecht: Springer Netherlands, 2013. http://dx.doi.org/10.1007/978-94-007-7735-4_3.

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Bateman, Andrew, Babykumari P. Chitramuthu, and Hugh P. J. Bennett. "Chromatographic Methods for the Purification of Granulin Peptides." In Methods in Molecular Biology, 19–34. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-8559-3_2.

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Mchedlishvili, B. V., E. Yu Morgunova, and A. M. Mikhailov. "Chromatographic Methods of Purification and Crystallization of Spherical Viruses." In Growth of Crystals, 181–96. Boston, MA: Springer US, 1991. http://dx.doi.org/10.1007/978-1-4615-3662-8_13.

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Cases, Barbara, Carlos Pastor-Vargas, and Marina Perez-Gordo. "Allergen Extraction and Purification from Natural Products: Main Chromatographic Techniques." In Methods in Molecular Biology, 13–22. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-6925-8_2.

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Ball, H. L., S. B. H. Kent, and P. Mascagni. "Selective purification of large synthetic peptides using removable chromatographic probes." In Peptides 1990, 323–25. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3034-9_137.

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Chaubal, Mahesh V., Kyung A. Kang, Sriram S. Tadepalli, William N. Drohan, and Duane F. Bruley. "Chromatographic Process Identification for Protein C Purification Using Frequency Response Analysis." In Advances in Experimental Medicine and Biology, 411–18. Boston, MA: Springer US, 1997. http://dx.doi.org/10.1007/978-1-4615-5865-1_53.

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Pérez, N., P. Rodríguez, L. Hernández, E. Muñoz, D. R. Orta, and S. Pérez. "Evaluation of Affinity Chromatographic Methods in the Purification of Recombinant Streptokinase." In Advances in Bioprocess Engineering, 535–40. Dordrecht: Springer Netherlands, 1994. http://dx.doi.org/10.1007/978-94-017-0641-4_74.

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Тези доповідей конференцій з теми "Chromatographic purification"

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Duesberg, G. S., J. Muster, V. Krstic, M. Burghard, and S. Roth. "Chromatographic purification and size separation of carbon nanotubes." In The 12th international winterschool on electronic properties of novel materials: progress in molecular nanostructures. AIP, 1998. http://dx.doi.org/10.1063/1.56531.

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Electricwala, A., and T. Atkinson. "TANDEM PURIFICATION OF TISSUE PLASMINOGEN ACTIVATOR BY METAL CHELATE AND AFFINITY CHROMATOGRAPHY." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644831.

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A tandem purification procedure was developed by a combination of metal chelate and affinity chromatography. The conditioned medium from different cell lines producing tissue plasminogen activator was first chromatographed on a zinc chelate-agarose column equilibrated with low ionic strength buffer. After thorough washing, the column was connected to a lysine-agarose column, previously equilibrated with the same buffer. Tissue plasminogen activator was eluted from the zinc chelate column by a gradient of imidazole and the effluent was allowed to flow through lysine-agarose matrix. The two columns were disconnected and after thorough washing, the bound enzyme from lysine-agarose column was eluted with a linear gradient of potassium thiocyanate in the equilibration buffer. This method resulted in a purification factor which varied between 40 to 110 fold. The purity of the isolated enzyme was assessed by sodium dodecyl sulphate-gel electrophoresis and fibrin zymography. The chromatographic procedure described provides a novel method for the rapid purification of tissue plasminogen activator to a high degree of purity.
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3

"Improvised Two-step Elution of Chromatographic Purification of Grouper’s Iridovirus Plasmid-based Vaccine by Monolithic Adsorbent." In International Conference on Advances in Science, Engineering, Technology and Natural Resources. International Institute of Chemical, Biological & Environmental Engineering, 2015. http://dx.doi.org/10.15242/iicbe.c0815057.

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Kempfer, A. C., N. Maugeri, C. Farías, E. Bermejo, M. Gimeno, and M. Lazzari. "PURIFICATION AND PARTIAL CHARACTERIZATION OF A BIOACTIVE SUBSTANCE FROM RAT'S VESSEL WALL INDEPENDENT OF PROSTACYCLIN PRODUCTION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643362.

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Our previous observations provided evidence that a bioactive substance (BAS) with inhibitory effect on platelet aggregation and with inotropic activity on smooth muscle preparations is present in aortic wall of rats treated previously with indomethacin. The ability to inhibit platelet aggregation was used for monitoring its purification and partial characterization. The original sample was extracted by rinsing aortic rings (1.5 mg dried rings) in buffer Krebs (300 μl) for 40 minutes at room temperature. The substance was purified by gel filtration (Bio-gel P-30, Sephadex G-100, Sephadex G-75) and ion exchange chromagra-phy (DEAE cellulose). In the last method, salt gradient elution was performed. Further purification by Sephadex G-50 resulted in removal of 90% of the contaminating substances without a loss of inhibitory activity. The main peak of both chromatographic procedures was analyzed on SDS-PAGE and PAGE with denaturing solvents. The substance was evident by Coomassie Brilliant Blue and periodic acid Schiff staining.In order to determine if the BAS was susceptible to proteolysis, an aliquot of the original sample (29 ug total protein) was incubated with trypsin (final concentration 0.3 μg/ml) and with chymotrypsin (final concentration 3 μg/ml). The BAS activity was not detected. An aliquot of the same original sample was incubated with neuraminidase (final concentration 1.2 units). The BAS activity was detected.The substance appeared to be stable for at least 18 hours at room temperature and 2 hours at 37°C, In addition it was stable over a pH range between 6.8 to 8.6, showing an anionic behaviour.The protein concentration of this substance determined by the method of Lowry was 1 μg/mlPartial characterization supports the conclusion that the substance present in aortic wall of rats is a homogeneous protein, which has a molecular size estimated at 55-65 kDa.
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5

Dyr, J. E., H. Fořtová, J. Suttnar, Z. Vorlová, and F. Kornalxk. "ISOLATION OF HUMAN PROTEIN C AND ITS SNAKE VENOM ACTIVATORS BY ION EXCHANGE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644896.

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Simple and efficient methods for the purification of functionally active clotting factors in good yields are still missing. The purpose of the present study was to design a chromatographic procedure for the isolation of protein C (PC) and its snake venom activators taking advantage of the high resolution, high speed of analysis and sensitive detection of high performance liquid chromatography.PC was purified from a human plasma concentrate containing vitamin Kdependent proteins using a Mono Q anion exchanger. Electrophoretic titration curve was used to serve as a guide for finding approximate conditions for separations. Elution profiles for vitamin K-dependent proteins were determined. PC was assayed by both immunological and functional methods. For the latter methods, protein C activators (PCA) were isolated from snake venoms of Agkistrodon c, -contortrix (ACC) and Agkistrodon c, mokasen.Both venoms (pooled samples)were found to contain at least two different PCA. AtpH 6.5> by simple one step procedures either an acidic PCA (on a Mono Q) or a basic PCA (on a Mono S) was isolated. A great diversity was found among venom samples from specimen originating from a small geographic area near Philadelphia (USA). In six out of the nine analysed ACC venoms only the acidic PCA was present.In conclusion, an optimum separationof protein C onthe Mono Q at pH 8.0 was proposed (usual recovery 90-95%).Optimalization of the salt gradient was considerably more effective than the pH changes. A great individual variability has to be taken into account when snake venoms are used as a source of protein C activators.
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6

Barredo, Gabriela R., Silvana L. Giudicessi, Mara C. Martnez-Ceron, Soledad L. Saavedra, Gustavo Mahler, Fernando Albericio, Osvaldo Cascone, and Silvia A. Camperi. "Bevacizumab Purification by Peptide Affinity Chromatography." In 35th European Peptide Symposium. Prompt Scientific Publishing, 2018. http://dx.doi.org/10.17952/35eps.2018.130.

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7

Takeya, H., S. Kawabata, T. Miyata, T. Morita, and S. Iwanaga. "A MODIFIED METHOD FOR PURIFICATION OF BOVINE FACTOR VII AND ITS PRIMARY STRUCTURE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643785.

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A modified method for purification of factor VII from bovine plasma was developed. The isolation procedures consisted of four steps with the ordinary barium citrate adsorption (1), DEAE-Sepharose chromatography (2), twice chromatographies on a benzamidine-Sepharose column (3) and affinity chromatography on Affigel-10 coupled with staphylocoagulase produced by Staphylococcus aureus, strain 213 (4). This final step was very effective for the removal of prothrombin contained in the pooled fraction of factor VII. Thus, these procedures allowed higher recovery of factor VII than the earlier methods and about 7 mg of the material was obtained from 15 liters of plasma. The purified preparation gave a single band on SDS-PAGE in the absence and presence of 2-mercaptoethanol and the apparent Mr was estimated as 53,000.To establish the whole primary structure at protein level, the isolated single chain factor VII was incubated with bovine factor Xlla and the resulting two chains-factor VII was reduced and S-pyridylethylated. The S-alkylated heavy and light chains were then separated on a TSK gel G3000SW followed by reversed phase HPLC on a Phenyl-5PWRP column. The amino acid sequence of the isolated light chain was determined by sequencing the peptides obtained from lysyl endopeptidase and α-chymotrypsin digests and from trypsin digest of the succinylated light chain. The light chain consisted of the total of 152 residues with 10 r-carboxyglutamic acids and contained one oligosaccharide chain at Asn-145. The light chain sequence was compared with that predicted from the cDNA sequence for human factor VII. It had 76 % sequence identity with the human's. The sequence of the factor Vll-heavy chain is being studied
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8

Lahoutifard-Henry, N., L. Pahnke, C. Le Quémener, G. Audo, and L. Simdon. "Centrifugal partition chromatography for purification of Cannabidiol from Cannabis sativa." In Phytotherapiekongress 2019. Georg Thieme Verlag KG, 2019. http://dx.doi.org/10.1055/s-0039-1697319.

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9

Masuda, Taisuke, Miyako Niimi, Kunihiro Kaihatsu, Nobuo Kato, and Fumihito Arai. "Purification of virus particles by ceramic hydroxyapatite chromatography on microfluidic chip." In 2014 IEEE 14th International Conference on Nanotechnology (IEEE-NANO). IEEE, 2014. http://dx.doi.org/10.1109/nano.2014.6968054.

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10

Li, Zhi-Hua, Reng-Qiang Li, and Man-Hua Liu. "Purification of Immunoglobulin from Rabbit Serum Using Strong Anion-exchange Chromatography." In 2015 International Conference on Medicine and Biopharmaceutical. WORLD SCIENTIFIC, 2016. http://dx.doi.org/10.1142/9789814719810_0089.

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Звіти організацій з теми "Chromatographic purification"

1

Wooley, R. J. Continuous countercurrent chromatographic separator for the purification of sugars from biomass hydrolyzate. Final project report, July 1, 1996--September 30, 1997. Office of Scientific and Technical Information (OSTI), December 1997. http://dx.doi.org/10.2172/563823.

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2

Warren, H. S. Purification of LPS Binding Factors in Tolerant Serum by Affinity Chromatography. Fort Belvoir, VA: Defense Technical Information Center, March 1991. http://dx.doi.org/10.21236/ada233638.

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3

Salmon, Arielle. Improving the Elution Rate of Extraction Chromatography on the Purification of Americium. Office of Scientific and Technical Information (OSTI), November 2018. http://dx.doi.org/10.2172/1484606.

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4

Barefoot, Susan F., Bonita A. Glatz, Nathan Gollop, and Thomas A. Hughes. Bacteriocin Markers for Propionibacteria Gene Transfer Systems. United States Department of Agriculture, June 2000. http://dx.doi.org/10.32747/2000.7573993.bard.

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The antibotulinal baceriocins, propionicin PLG-1 and jenseniin G., were the first to be identified, purified and characterized for the dairy propionibaceria and are produced by Propionibacterium thoenii P127 and P. thoenii/jensenii P126, respectively. Objectives of this project were to (a) produce polyclonal antibodies for detection, comparison and monitoring of propionicin PLG-1; (b) identify, clone and characterize the propionicin PLG-1 (plg-1) and jenseniin G (jnG) genes; and (3) develop gene transfer systems for dairy propionibacteria using them as models. Polyclonal antibodies for detection, comparison and monitoring of propionicin PLG-1 were produced in rabbits. Anti-PLG-1 antiserum had high titers (256,000 to 512,000), neutralized PLG-1 activity, and detected purified PLG-1 at 0.10 mg/ml (indirect ELISA) and 0.033 mg/ml (competitive indirect ELISA). Thirty-nine of 158 strains (most P. thoenii or P. jensenii) yielded cross-reacting material; four strains of P. thoenii, including two previously unidentified bacteriocin producers, showed biological activity. Eight propionicin-negative P127 mutants produced neither ELISA response nor biological activity. Western blot analyses of supernates detected a PLG-1 band at 9.1 kDa and two additional protein bands with apparent molecular weights of 16.2 and 27.5 kDa. PLG-1 polyclonal antibodies were used for detection of jenseniin G. PLG-1 antibodies neutralized jenseniin G activity and detected a jenseniin G-sized, 3.5 kDa peptide. Preliminary immunoprecipitation of crude preparations with PLG-1 antibodies yielded three proteins including an active 3-4 kDa band. Propionicin PLG-1 antibodies were used to screen a P. jensenii/thoenii P126 genomic expression library. Complete sequencing of a cloned insert identified by PLG-1 antibodies revealed a putative response regulator, transport protein, transmembrane protein and an open reading frame (ORF) potentially encoding jenseniin G. PCR cloning of the putative plg-1 gene yielded a 1,100 bp fragment with a 355 bp ORF encoding 118 amino acids; the deduced N-terminus was similar to the known PLG-1 N-terminus. The 118 amino acid sequence deduced from the putative plg-1 gene was larger than PLG-1 possibly due to post-translational processing. The product of the putative plg-1 gene had a calculated molecular weight of 12.8 kDa, a pI of 11.7, 14 negatively charged residues (Asp+Glu) and 24 positively charged residues (Arg+Lys). The putative plg-1 gene was expressed as an inducible fusion protein with a six-histidine residue tag. Metal affinity chromatography of the fused protein yielded a homogeneous product. The fused purified protein sequence matched the deduced putative plg-1 gene sequence. The data preliminarily suggest that both the plg-1 and jnG genes have been identified and cloned. Demonstrating that antibodies can be produced for propionicin PLG-1 and that those antibodies can be used to detect, monitor and compare activity throughout growth and purification was an important step towards monitoring PLG-1 concentrations in food systems. The unexpected but fortunate cross-reactivity of PLG-1 antibodies with jenseniin G led to selective recovery of jenseniin G by immunoprecipitation. Further refinement of this separation technique could lead to powerful affinity methods for rapid, specific separation of the two bacteriocins and thus facilitate their availability for industrial or pharmaceutical uses. Preliminary identification of genes encoding the two dairy propionibacteria bacteriocins must be confirmed; further analysis will provide means for understanding how they work, for increasing their production and for manipulating the peptides to increase their target species. Further development of these systems would contribute to basic knowledge about dairy propionibacteria and has potential for improving other industrially significant characteristics.
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