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Journal articles on the topic 'Chromatographic purification'

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Published: 30 May 2022

Last updated: 31 May 2022

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1

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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6

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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7

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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8

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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9

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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10

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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11

Henneberg, Fabian, and Ashwin Chari. "Chromatography-Free Purification Strategies for Large Biological Macromolecular Complexes Involving Fractionated PEG Precipitation and Density Gradients." Life 11, no. 12 (November 24, 2021): 1289. http://dx.doi.org/10.3390/life11121289.

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A complex interplay between several biological macromolecules maintains cellular homeostasis. Generally, the demanding chemical reactions which sustain life are not performed by individual macromolecules, but rather by several proteins that together form a macromolecular complex. Understanding the functional interactions amongst subunits of these macromolecular machines is fundamental to elucidate mechanisms by which they maintain homeostasis. As the faithful function of macromolecular complexes is essential for cell survival, their mis-function leads to the development of human diseases. Furthermore, detailed mechanistic interrogation of the function of macromolecular machines can be exploited to develop and optimize biotechnological processes. The purification of intact macromolecular complexes is an essential prerequisite for this; however, chromatographic purification schemes can induce the dissociation of subunits or the disintegration of the whole complex. Here, we discuss the development and application of chromatography-free purification strategies based on fractionated PEG precipitation and orthogonal density gradient centrifugation that overcomes existing limitations of established chromatographic purification protocols. The presented case studies illustrate the capabilities of these procedures for the purification of macromolecular complexes.

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12

Medda, Rosaria, Francesca Pintus, Delia Spanò, and Giovanni Floris. "Bioseparation of Four Proteins fromEuphorbia characiasLatex: Amine Oxidase, Peroxidase, Nucleotide Pyrophosphatase/Phosphodiesterase, and Purple Acid Phosphatase." Biochemistry Research International 2011 (2011): 1–7. http://dx.doi.org/10.1155/2011/369484.

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This paper deals with the purification of four proteins fromEuphorbia characiaslatex, a copper amine oxidase, a nucleotide pyrophosphatase/phosphodiesterase, a peroxidase, and a purple acid phosphatase. These proteins, very different in molecular weight, in primary structure, and in the catalyzed reaction, are purified using identical preliminary steps of purification and by chromatographic methods. In particular, the DEAE-cellulose chromatography is used as a useful purification step for all the four enzymes. The purification methods here reported allow to obtain a high purification of all the four proteins with a good yield. This paper will give some thorough suggestions for researchers busy in separation of macromolecules from different sources.

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13

Brämer, Chantal, Lisa Tünnermann, Alina Gonzalez Salcedo, Oscar-Werner Reif, Dörte Solle, Thomas Scheper, and Sascha Beutel. "Membrane Adsorber for the Fast Purification of a Monoclonal Antibody Using Protein A Chromatography." Membranes 9, no. 12 (November 27, 2019): 159. http://dx.doi.org/10.3390/membranes9120159.

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Monoclonal antibodies are conquering the biopharmaceutical market because they can be used to treat a variety of diseases. Therefore, it is very important to establish robust and optimized processes for their production. In this article, the first step of chromatography (Protein A chromatography) in monoclonal antibody purification was optimized with a focus on the critical elution step. Therefore, different buffers (citrate, glycine, acetate) were tested for chromatographic performance and product quality. Membrane chromatography was evaluated because it promises high throughputs and short cycle times. The membrane adsorber Sartobind® Protein A 2 mL was used to accelerate the purification procedure and was further used to perform a continuous chromatographic run with a four-membrane adsorber-periodic counter-current chromatography (4MA-PCCC) system. It was found that citrate buffer at pH 3.5 and 0.15 M NaCl enabled the highest recovery of >95% and lowest total aggregate content of 0.26%. In the continuous process, the capacity utilization of the membrane adsorber was increased by 20%.

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14

Riesco, O. F., S. Hajri-Mezghani, and S. Z. Cekan. "Estimation of true values in radioimmunoassays." Clinical Chemistry 35, no. 8 (August 1, 1989): 1680–83. http://dx.doi.org/10.1093/clinchem/35.8.1680.

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Abstract We tested the accuracy of radioimmunoassays for two hormones, progesterone and estradiol, in relation to the use of two different antisera in each assay and to the degree of purification from plasma before the assay was done. Each analyte was assayed either in a diethyl ether extract, in a zone eluted from a Sephadex LH-20 chromatographic column, or in fractions of a chromatographic zone (from Sephadex LH-20 or Celite) that passed a test of "radiochemical purity." Statistically indistinguishable results were obtained in the assay of radiochemically pure fractions of both analytes, irrespective of the antiserum used. In addition, one of the antisera from each hormone gave equivalent results in the radioimmunoassay of ether extracts, even with no preceding chromatography. We demonstrated in this way that results obtained with use of highly specific antisera may, after a single chromatography, but even without any chromatographic purification, be as nearly accurate and as closely reflect the true value as those obtained in the assay of radiochemically pure hormones, an assay that has a character of a reference method (as defined by the IFCC).

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15

Chao, Allen, Embarek Alwedi, and Fraser Fleming. "Isocyanide Purification: C-2 Silica Cleans Up a Dirty Little Secret." Synthesis 51, no. 10 (February 18, 2019): 2122–27. http://dx.doi.org/10.1055/s-0037-1611719.

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EtSiCl3-treated silica gel, ‘C-2 silica,’ proved exceptionally effective for purifying isocyanides that are otherwise irreversibly adsorbed during silica gel chromatography. Purification of a prototypical isocyanide on several chromatographic matrices provided valuable insight into the requirements for purifying silica-sensitive isocyanides. EtSiCl3-modified silica proved optimal as the solid phase, providing up to 90% recovery of pure isocyanides that otherwise fail to elute during silica gel purification.

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16

Endre, Gábor, Zsófia Hegedüs, Adiyadolgor Turbat, Biljana Škrbić, Csaba Vágvölgyi, and András Szekeres. "Separation and Purification of Aflatoxins by Centrifugal Partition Chromatography." Toxins 11, no. 6 (May 30, 2019): 309. http://dx.doi.org/10.3390/toxins11060309.

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Aflatoxins are mycotoxins that are produced by several species of filamentous fungi. In the European Union, the concentration limits for this group of mycotoxins in food and feed products are very low (on the order of parts per billion). Thus, relatively high amounts of these substances in their pure forms are required as reference standards. Chromatographic techniques based on solid stationary phases are generally used to purify these molecules; however, liquid–liquid chromatographic separations may be a promising alternative. Therefore, this study proposes a liquid–liquid chromatographic method for the separation of four aflatoxins and impurities. To optimise the method, numerous biphasic solvent systems (chloroform-, acetone- and acetic acid-based systems) were tested and evaluated in terms of their effectiveness at partitioning aflatoxins; the toluene/acetic acid/water (30:24:50, v/v/v/%) system was found to be the most efficient for application in centrifugal partition chromatographic instrument. Using liquid–liquid instrumental separation, the four aflatoxins, namely B1 (400 mg), B2 (34 mg), G1 (817 mg) and G2 (100 mg), were successfully isolated with 96.3%–98.2% purity from 4.5 L of Aspergillus parasiticus fermented material in a 250 mL centrifugal partition chromatography column. The identities and purities of the purified components were confirmed, and the performance parameters of each separation step and the whole procedure was determined. The developed method could be effectively used to purify aflatoxins for analytical applications.

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17

Mestmäcker, Fabian, Axel Schmidt, Maximilian Huter, Maximilian Sixt, and Jochen Strube. "Systematic and Model-Assisted Process Design for the Extraction and Purification of Artemisinin from Artemisia annua L.—Part III: Chromatographic Purification." Processes 6, no. 10 (October 2, 2018): 180. http://dx.doi.org/10.3390/pr6100180.

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In this study, the purification of an extract from Artemisia annua L. using chromatographic methods is studied. In a first step, a screening of different phases and solvents using thin-layer chromatography (TLC) was performed. Then, a laboratory-scale high performance liquid chromatography (HPLC) method was developed and transferred to a pilot scale. A reproducibility study based on 120 injections was carried out. The batch process that was developed and the results from a designed continuous simulated moving bed (SMB) chromatography were compared based on characteristic process numbers and economy.

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18

Jao, Yun, Wu-Long Cheng, and Gann Ting. "Chromatographic separation and purification of Xenon-133." Journal of Chromatography A 462 (January 1989): 191–204. http://dx.doi.org/10.1016/s0021-9673(00)91347-5.

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19

Kovář, J., and J. Stejskal. "Rapid chromatographic purification of yeast alcohol dehydrogenase." Journal of Chromatography A 325 (January 1985): 359–62. http://dx.doi.org/10.1016/s0021-9673(00)96044-8.

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20

Pasechnik, V. A. "Chromatographic methods for purification of leukocyte interferon." Journal of Chromatography A 364 (September 1986): 359–68. http://dx.doi.org/10.1016/s0021-9673(00)96226-5.

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21

Ebright, Yon, Guillermo I. Tous, Jonglin Tsao, Jodi Fausnaugh, and Stanley Stein. "Chromatographic Purification of Non-Ionic Methylphosphonate Oligodeoxyribonucleosides." Journal of Liquid Chromatography 11, no. 9-10 (July 1988): 2005–17. http://dx.doi.org/10.1080/01483918808069037.

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22

FUNK, M. O., Y. NAKAGAWA, J. SKOCHDOPOLE, and E. T. KAISER. "AFFINITY CHROMATOGRAPHIC PURIFICATION OF PAPAIN A Reinvestigation." International Journal of Peptide and Protein Research 13, no. 3 (January 12, 2009): 296–303. http://dx.doi.org/10.1111/j.1399-3011.1979.tb01883.x.

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23

STROBEL, R., and M. ROSENBERG. "Immunoaffinity Chromatographic Purification of Chicken ectoATP Diphosphohydrolase." Annals of the New York Academy of Sciences 671, no. 1 Ion-Motive AT (November 1992): 487–89. http://dx.doi.org/10.1111/j.1749-6632.1992.tb43837.x.

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24

Heinonen, Jari, Henna Niskakoski, Baoru Yang, Maaria Kortesniemi, and Tuomo Sainio. "Chromatographic purification of enzymatically synthesized alkyl glucopyranosides." Journal of Chemical Technology & Biotechnology 91, no. 9 (November 9, 2015): 2419–31. http://dx.doi.org/10.1002/jctb.4830.

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25

Rathore, Anurag S., Devashish Kumar, and Nikhil Kateja. "Recent developments in chromatographic purification of biopharmaceuticals." Biotechnology Letters 40, no. 6 (April 27, 2018): 895–905. http://dx.doi.org/10.1007/s10529-018-2552-1.

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26

Bajpai, Vivek K., Rajib Majumder, and Jae Gyu Park. "Isolation and purification of plant secondary metabolites using column-chromatographic technique." Bangladesh Journal of Pharmacology 11, no. 4 (October 1, 2016): 844. http://dx.doi.org/10.3329/bjp.v11i4.28185.

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<p>Chromatographic techniques have significant role in natural products chemistry as well as contribute dramatically in the discovery of novel and innovative compounds of pharmaceutical and biomedical importance. This study focused on step-by-step visual demonstration of fractionation and isolation of biologically active plant secondary metabolites using column-chromatographic techniques. Isolation of bioactive compounds using column-chromatographic involves: a) Preparation of sample; b) Packing of column; c) Pouring of sample into the column; d) Elution of fractions; and e) Analysis of each fractions using thin layer chromatography. However, depending on nature of research, compounds can be further purified using high performance liquid chromatography (HPLC), and nuclear magnetic resonance (NMR) spectral analyses.</p><p><strong>Video Clips</strong></p><p><a href="https://www.youtube.com/v/pr8mrBoI8xA">Part 1:</a> 3 min 45 sec</p><p><a href="https://www.youtube.com/v/rYrfClKn-og">Part 2:</a> 6 min 21 sec</p><p><a href="https://www.youtube.com/v/kffHXxuPwbo">Part 3</a>: 4 min 45 sec</p>

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27

Lau, Eric C., Damian J. Mason, Nicole Eichhorst, Pearce Engelder, Celestina Mesa, E. M. Kithsiri Wijeratne, G. M. Kamal B. Gunaherath, A. A. Leslie Gunatilaka, James J. La Clair, and Eli Chapman. "Functional chromatographic technique for natural product isolation." Organic & Biomolecular Chemistry 13, no. 8 (2015): 2255–59. http://dx.doi.org/10.1039/c4ob02292k.

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28

Igumnov, Sergey N., Vladimir N. Kulagin, and Tatyana B. Korneeva. "Purification of Acetonitrile." Advanced Materials Research 560-561 (August 2012): 202–6. http://dx.doi.org/10.4028/www.scientific.net/amr.560-561.202.

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The procedure is described for the purification of acetonitrile to a level suitable for spectroscopic and chromatographic work. Rectification of chemical pretreated acetonitrile was performed on glass vacuum-jacketed column, filled with spiral-prismatic packing.

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29

Mali, S. D., and A. P. Jadhav. "EXTRACTION AND ISOLATION OF EMBELIN USING FLASH CHROMATOGRAPHY." INDIAN DRUGS 53, no. 06 (June 28, 2016): 80–81. http://dx.doi.org/10.53879/id.53.06.10443.

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A rapid and efficient flash chromatographic process for selective isolation of embelin from Embelia ribes was developed. The rate of extraction and purity of embelin depends upon the solvent used for extraction and optimized chromatographic separation. Ethyl acetate was found to be best solvent for highest possible recovery of the embelin from Embelia ribes. Flash chromatography speed up the purification process for quicker results. The purified sample of embelin was then characterized by UV, HPTLC, NMR and Mass.

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30

Mohammad, Abdul Wahab, Jamaliah Md.Jahim, Suhaila Johar, and Osman Hassan. "Comparison of Cutinase Separation in Different Chromatographic Media." ASEAN Journal of Chemical Engineering 12, no. 2 (February 7, 2013): 11. http://dx.doi.org/10.22146/ajche.49738.

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Cutinase is a hydrolytic enzyme that has both properties of lipase and esterase, thus finding its use in many areas. Previous studies have investigated both upstream and downstream processes for cutinase production from microbial source. However, no study has yet to address the use of membrane chromatography for cutinase purification, which is more favourable in terms of process resolution and product throughput as compared to the conventional gel chromatography. Hydrophobic interaction was chosen as the separation mechanism for cutinase purification in this study. The optimisation of cutinase purification in two different types of chromatographic media; conventional packed-gel and membrane matrix, were pre-determined by the best compromise between the recovery and purity of the purified cutinase. It was found that the optimised condition were of pH 4.0 and 1.0 M ammonium sulfate for the conventional column (50% recovery, 4.8-fold purity) and pH 6.0 with 1.5 M ammonium sulfate for the membrane–matrix column(87% recovery, 30-fold purity). Preferential interaction analysis was used to describe the protein chromatographic behaviour in each chromatographic media. Graph of natural algorithm of protein retention data to the function of salt concentration at pH 4.0 and 6.0 for each column were plotted. It was found that at the optimum pH condition for gel-packed column, a small amount of ammonium sulfate was sufficient to achieve maximum cutinase recovery and purity since the effect of salt at that particular pH were less significant. Consequently, the number of released water molecules were calculated and it was observed that for membrane column, larger number of water was released at pH 6.0 illustrating more protein were bounded to the stationary phase, thus explaining the optimum pH condition of the particular column.

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31

He, Xuemei M., Carsten Voß, and Jidong Li. "Exploring the Unique Selectivity of Hydrophobic Cation Exchanger Nuvia cPrime for the Removal of a Major Process Impurity: A Case Study with IgM." Current Protein & Peptide Science 20, no. 1 (November 9, 2018): 65–74. http://dx.doi.org/10.2174/1389203718666171017130506.

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Background: Mixed-mode chromatography is becoming an important tool for downstream process purification, as it provides the selectivity and robustness unmatched by conventional singlemode chromatographic methods. The joint action of multiple functionalities present on the ligands of mixed-mode chromatography matrices effectively enhances the separation of target molecules from impurities. Material and Methods: Using Nuvia cPrime as an example, we elucidate the separation principles of hydrophobic cation exchange mixed-mode chromatography and its difference from traditional strong cation exchangers. We have developed a Nuvia cPrime based polish purification step specifically for the removal of a major process contaminant, which has an isoelectric point similar to that of the target monoclonal IgM molecule. Additional purification was accomplished using a second mixed-mode chromatography column packed with Ceramic Hydroxyapatite. Conclusion: The monoclonal IgM prepared with this new process fully retained its biological activity and was free of high molecular weight aggregates, a product quality that was not achievable in previous attempts using traditional ion exchange or hydrophobic interaction chromatography.

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32

Leznoff, Clifford C., Colin R. McArthur, and Yongnian Qin. "Phthalocyanine-modified silica gels and their application in the purification of unsymmetrical phthalocyanines." Canadian Journal of Chemistry 71, no. 9 (September 1, 1993): 1319–26. http://dx.doi.org/10.1139/v93-170.

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Five species of phthalocyanine-modified silica gels were prepared. The loadings of phthalocyanine on these silica gels were determined by acidic hydrolysis. The concept of using the aggregation phenomenon to advantage to aid chromatographic separation of unsymmetrical phthalocyanines was investigated by employing these modified silica gels as chromatographic media to purify unsymmetrical phthalocyanines. Four groups of phthalocyanine mixtures were prepared by mixed condensation. One of the desired unsymmetrical phthalocyanines was successfully purified by conventional column chromatography while others were separated by the new method described herein.

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33

Swanson, Steven P., Andrew M. Dahlem, Harold D. Rood, Louis-Marie Côte, William B. Buck, and Takumi Yoshizawa. "Gas Chromatographic Analysis of Milk for Deoxynivalenol and Its Metabolite DOM-1." Journal of AOAC INTERNATIONAL 69, no. 1 (January 1, 1986): 41–43. http://dx.doi.org/10.1093/jaoac/69.1.41.

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Abstract A gas chromatographic method is described for the determination of deoxynivalenol (DON) and its metabolite DOM-1 in milk. Milk samples were extracted with ethyl acetate on a commercially available disposable extraction column, followed by hexane-acetonitrile partitioning. Final purification was accomplished on a reverse phase C-18 cartridge. The trimethylsilyl ether (TMS) derivatives of DON were prepared, chromatographed on an OV-17 column, and quantitated with an electron capture detector. Chromatography of the TMS derivatives of milk extracts was compared to that of the corresponding heptafluorobutyryl derivatives. The limit of detection using TMS derivatives was 1 ng/mL for both toxins with recoveries averaging 82% ± 9% at 2.5 and 10 ng/ mL milk for DON and 85% ± 6% at 10 ng/mL for DOM-1.

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34

Nyiredy, Szabolcs. "The Role of Planar Chromatography in Medicinal Plant Research." Journal of AOAC INTERNATIONAL 84, no. 4 (July 1, 2001): 1219–31. http://dx.doi.org/10.1093/jaoac/84.4.1219.

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Abstract This paper summarizes the role of planar chromatography (PC) in medicinal and aromatic plant (MAP) research and development, and demonstrates the importance of the technique, after extraction, in the analysis of MAP (identification and quantitative determination of the separated compound/s), in the purification and isolation process, and in different types of screening procedure. Special attention is paid to analytical, micropreparative and preparative forced-flow techniques, for example overpressured-layer chromatography (OPLC) and rotation planar chromatography (RPC). The special features of analytical, micropreparative, and preparative layer chromatography (PLC), OPLC, and RPC are compared in tables. Purification and isolation procedures using forced-flow techniques are shown in flowcharts. Some applications, relating to different classes of substance, are presented to demonstrate the versatility of various planar chromatographic techniques.

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35

Lebedev, L. R., Е. А. Volosnikova, I. P. Gileva, Ya S. Gogina, Т. А. Tereshchenko, G. V. Kochneva, A. A. Grazhdantseva, and E. D. Danilenko. "Method for Obtaining Recombinant Human Granulocyte-Macrophage Colony-Stimulating Factor." Biotekhnologiya, no. 3 (2019): 68–73. http://dx.doi.org/10.21519/0234-2758-2019-35-3-68-73.

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A suggested method for obtaining recombinant human granulocyte-macrophage colony-stimulating factor (GM-CSF) includes the accumulation of the producer strain biomass enriched with the target product up to 30% of total protein content, its isolation and purification. The later consists of the following stages: ultrasound cell disintegration, washing of inclusion bodies with buffer solutions, GM-CSF solubilization from inclusion bodies by 6 M urea, denaturation-renaturation of protein molecules and purification by chromatography on DEAE-Sepharose and combined chromatography on CM-Sepharose and Q-Sepharose followed by dialysis. The proposed method makes it possible to yield up to 10 mg of the protein preparation from 1 g of wet cells with the purity of 98% and high activity shown on the human erythroleukemia cell line. granulocyte-macrophage colony-stimulating, GM-CSF, producer strain, cultivation, chromatographic purification. The work was performed in the framework of the State Assignment «Adjustment of the Technology of Preparative Obtaining and Purification of Recombinant Proteins» (no. 13/18).

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36

Wu, Yuteng, Alessandro Zorzi, Jack Williams, and Christian Heinis. "A releasable disulfide-linked peptide tag facilitates the synthesis and purification of short peptides." Chemical Communications 56, no. 19 (2020): 2917–20. http://dx.doi.org/10.1039/c9cc09247a.

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37

Bernardo, Sandra C., Rita Carapito, Márcia C. Neves, Mara G. Freire, and Fani Sousa. "Supported Ionic Liquids Used as Chromatographic Matrices in Bioseparation—An Overview." Molecules 27, no. 5 (February 28, 2022): 1618. http://dx.doi.org/10.3390/molecules27051618.

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Liquid chromatography plays a central role in biomanufacturing, and, apart from its use as a preparative purification strategy, either in biopharmaceuticals or in fine chemicals industries, it is also very useful as an analytical tool for monitoring, assessing, and characterizing diverse samples. The present review gives an overview of the progress of the chromatographic supports that have been used in the purification of high-value products (e.g., small molecules, organic compounds, proteins, and nucleic acids). Despite the diversity of currently available chromatographic matrices, the interest in innovative biomolecules emphasizes the need for novel, robust, and more efficient supports and ligands with improved selectivity. Accordingly, ionic liquids (ILs) have been investigated as novel ligands in chromatographic matrices. Given herein is an extensive review regarding the different immobilization strategies of ILs in several types of supports, namely in silica, Sepharose, and polymers. In addition to depicting their synthesis, the main application examples of these supports are also presented. The multiple interactions promoted by ILs are critically discussed concerning the improved selectivity towards target molecules. Overall, the versatility of supported ILs is here considered a critical point to their exploitation as alternatives to the more conventional liquid chromatographic matrices used in bioseparation processes.

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38

Oksanen, Hanna M., Ausra Domanska, and Dennis H. Bamford. "Monolithic ion exchange chromatographic methods for virus purification." Virology 434, no. 2 (December 2012): 271–77. http://dx.doi.org/10.1016/j.virol.2012.09.019.

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Schott, Herbert, Rolf Semmler, and Heiner Eckstein. "Column chromatographic purification of guanylate-rich synthetic oligodeoxyribonucleotides." Journal of Chromatography A 389 (January 1987): 165–76. http://dx.doi.org/10.1016/s0021-9673(01)94420-6.

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Wimmerovd, M., Z. Glatz, O. Janiczek, and L. Macholdn. "Improved Chromatographic Purification of Pea Seedlings Diamine Oxidase." Preparative Biochemistry 23, no. 3 (January 1993): 303–19. http://dx.doi.org/10.1080/10826069308544558.

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Akiba, Kenichi, Hiroyuki Hashimoto, Akira Tsuyoshi, and Shigeto Nakamura. "HIGH-SPEED COUNTERCURRENT CHROMATOGRAPHIC PURIFICATION OF MIDDLE LANTHANOIDS." Journal of Liquid Chromatography & Related Technologies 22, no. 18 (January 1999): 2795–805. http://dx.doi.org/10.1081/jlc-100102059.

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Brunner, G., F. Tegtmeier, D. N. Kirk, S. Wynn, and K. D. R. Setchell. "Enzymatic synthesis and chromatographic purification of lignan glucuronides." Biomedical Chromatography 1, no. 2 (April 1986): 89–92. http://dx.doi.org/10.1002/bmc.1130010207.

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Chapman, George E., Jackie Rott, John E. More, Peter A. Feldman, and Paul Matejtschuk. "Chromatographic purification of protein therapeutics: An industrial perspective." Journal of Chemical Technology AND Biotechnology 59, no. 1 (January 1994): 108–9. http://dx.doi.org/10.1002/jctb.280590122.

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Barroso, Telma, Abid Hussain, Ana C. A. Roque, and Ana Aguiar-Ricardo. "Functional monolithic platforms: Chromatographic tools for antibody purification." Biotechnology Journal 8, no. 6 (May 6, 2013): 671–81. http://dx.doi.org/10.1002/biot.201200328.

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Ferreira, G. N. M., J. M. S. Cabral, and D. M. F. Prazeres. "Purification of supercoiled plasmid DNA using chromatographic processes." Journal of Molecular Recognition 11, no. 1-6 (December 1998): 250–51. http://dx.doi.org/10.1002/(sici)1099-1352(199812)11:1/6<250::aid-jmr433>3.0.co;2-1.

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Sugo, Ken, and Tsuneo Okuyama. "Hydroxyapatite chromatographic procedures for phospholipids: Endotoxin purification methods." Separation Science and Technology 53, no. 10 (November 27, 2017): 1572–79. http://dx.doi.org/10.1080/01496395.2017.1397025.

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Zhao, Xinyu, Guoshun Li, and Shufang Liang. "Several Affinity Tags Commonly Used in Chromatographic Purification." Journal of Analytical Methods in Chemistry 2013 (2013): 1–8. http://dx.doi.org/10.1155/2013/581093.

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Affinity tags have become powerful tools from basic biological research to structural and functional proteomics. They were widely used to facilitate the purification and detection of proteins of interest, as well as the separation of protein complexes. Here, we mainly discuss the benefits and drawbacks of several affinity or epitope tags frequently used, including hexahistidine tag, FLAG tag, Strep II tag, streptavidin-binding peptide (SBP) tag, calmodulin-binding peptide (CBP), glutathione S-transferase (GST), maltose-binding protein (MBP), S-tag, HA tag, and c-Myc tag. In some cases, a large-size affinity tag, such as GST or MBP, can significantly impact on the structure and biological activity of the fusion partner protein. So it is usually necessary to excise the tag by protease. The most commonly used endopeptidases are enterokinase, factor Xa, thrombin, tobacco etch virus, and human rhinovirus 3C protease. The proteolysis features of these proteases are described in order to provide a general guidance on the proteolytic removal of the affinity tags.

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Gétaz, David, Guido Stroehlein, Alessandro Butté, and Massimo Morbidelli. "Model-based design of peptide chromatographic purification processes." Journal of Chromatography A 1284 (April 2013): 69–79. http://dx.doi.org/10.1016/j.chroma.2013.01.118.

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van Ginkel, L. A., E. H. J. M. Jansen, R. W. Stephany, P. W. Zoontjes, P. L. W. J. Schwillens, H. J. van Rossum, and T. Visser. "Liquid chromatographic purification and detection of anabolic compounds." Journal of Chromatography A 624, no. 1-2 (October 1992): 389–401. http://dx.doi.org/10.1016/0021-9673(92)85690-u.

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Gooding, David L., Mery Nell Schmuck, Mark P. Nowlan, and Karen M. Gooding. "Optimization of preparative hydrophobic interaction chromatographic purification methods." Journal of Chromatography A 359 (January 1986): 331–37. http://dx.doi.org/10.1016/0021-9673(86)80087-5.

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