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Journal articles on the topic 'Protein A chromatography'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Mikšı́k, Ivan. "Protein liquid chromatography." Journal of Chromatography B: Biomedical Sciences and Applications 749, no. 1 (November 2000): 143–44. http://dx.doi.org/10.1016/s0378-4347(00)00366-2.

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2

Janson, Jan-Christer. "Practical protein chromatography." Journal of Biochemical and Biophysical Methods 26, no. 2-3 (May 1993): 244–45. http://dx.doi.org/10.1016/0165-022x(93)90050-x.

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3

Cho, A.-Young, Giyoung Kim, Jongguk Lim, Changyeun Mo, Ji-Hea Moon, SaetByeol Park, Su-Hee Park, and Aeson Om. "Separation of Staphylococcal Enterotoxin B by Fast Protein Liquid Chromatography." Food Engineering Progress 19, no. 2 (May 31, 2015): 111–16. http://dx.doi.org/10.13050/foodengprog.2015.19.2.111.

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4

Brocklehurst, Keith, Albert J. Courey, Sheraz Gul, Sue-Hwa Lin, and Robert L. Moritz. "Protein Ligand Affinity Chromatography." Cold Spring Harbor Protocols 2006, no. 1 (January 1, 2006): pdb.prot4203. http://dx.doi.org/10.1101/pdb.prot4203.

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5

Geng, Xindu, and Lili Wang. "Liquid chromatography of recombinant proteins and protein drugs." Journal of Chromatography B 866, no. 1-2 (April 2008): 133–53. http://dx.doi.org/10.1016/j.jchromb.2008.01.041.

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6

Shukla, Abhinav A., Priyanka Gupta, and Xuejun Han. "Protein aggregation kinetics during Protein A chromatography." Journal of Chromatography A 1171, no. 1-2 (November 2007): 22–28. http://dx.doi.org/10.1016/j.chroma.2007.09.040.

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7

KRUGER, J. E., and B. A. MARCHYLO. "SELECTION OF COLUMN AND OPERATING CONDITIONS FOR REVERSED-PHASE HIGH-PERFORMANCE LIQUID CHROMATOGRAPHY OF PROTEINS IN CANADIAN WHEAT." Canadian Journal of Plant Science 65, no. 2 (April 1, 1985): 285–98. http://dx.doi.org/10.4141/cjps85-041.

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Chromatographic conditions were optimized and three commercially available columns were evaluated for separation of alcohol-soluble storage proteins of Neepawa wheat using reversed-phase high-performance liquid chromatography (RP-HPLC). Optimal separation was achieved using an extracting solution of 50% 1-propanol, 1% acetic acid, and 4% dithiothreitol and an HPLC elution time of 105 min at a flow rate of 1.0 mL/min. HPLC columns evaluated (SynChropak RP-P, Ultrapore RPSC and Aquapore RP-300) varied in selectivity and resolution. The column providing the greatest versatility was Aquapore RP-300 available in cartridge form. Sodium dodecyl sulfate gradient-gel electrophoresis analysis of protein peaks resolved by RP-HPLC indicated that many of the eluted peaks contained more than one protein species. Chromatographic protein patterns obtained for Neepawa wheat grown at different locations and in different years were qualitatively the same.Key words: Protein, high-performance liquid chromatography, wheat

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8

Holm, Jan, Steen Ingemann Hansen, and Mimi Høier-Madsen. "A Combination of Cation Exchange and Ligand-Affinity Chromatography for Purification of Two Molecular Species of the Folate Binding Protein in Human Milk, One Equipped with a Hydrophobic Glycosyl Phosphatidylinositol Tail: Characterization of Hydrophobicity and Electrical Charge." Bioscience Reports 22, no. 3-4 (August 1, 2002): 443–54. http://dx.doi.org/10.1023/a:1020922226362.

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Cation exchange chromatography combined with ligand (methotrexate) affinity chromatography on a column desorbed with a pH-gradient was used for separation and large scale purification of two folate binding proteins in human milk. One of the proteins, which had a molecular size of 27 kDa on gel filtration and eluted from the affinity column at pH 5–6 was a cleavage product of a 100 kDa protein eluted at pH 3–4 as evidenced by identical N-terminal amino acid sequences and a reduction in the molecular size of the latter protein to 27 kDa after cleavage of its hydrophobic glycosylphosphatidyl-inositol tail that inserts into Triton X-100 micelles. Chromatofocusing showed that both proteins possessed multiple isoelectric points within the pH range 7–9. The 100 kDa protein exhibited a high affinity to hydrophobic interaction chromatographic gels, whereas this was only the case with unliganded forms of the 27 kDa protein indicative of a decrease in the hydrophobicity of the protein after ligand binding.

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9

Cassidy, Scott A., Linda J. Janis, and Fred E. Regnier. "Kinetic chromatographic sequential addition immunoassays using protein A affinity chromatography." Analytical Chemistry 64, no. 17 (September 1992): 1973–77. http://dx.doi.org/10.1021/ac00041a036.

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10

Gottstein, C., and R. Forde. "Affinity chromatography system for parallel purification of recombinant protein samples." Protein Engineering, Design and Selection 15, no. 10 (October 2002): 775–77. http://dx.doi.org/10.1093/protein/15.10.775.

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11

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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12

Scouten, William H. "Affinity chromatography for protein isolation." Current Opinion in Biotechnology 2, no. 1 (February 1991): 37–43. http://dx.doi.org/10.1016/0958-1669(91)90059-e.

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13

Regnier, Fred E. "Chromatography of complex protein mixtures." Journal of Chromatography B: Biomedical Sciences and Applications 418 (July 1987): 115–43. http://dx.doi.org/10.1016/0378-4347(87)80007-5.

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14

Chaplin, L. C. "Hydrophobic interaction fast protein liquid chromatography of milk proteins." Journal of Chromatography A 363, no. 2 (January 1986): 329–35. http://dx.doi.org/10.1016/s0021-9673(01)83753-5.

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15

Muronetz, Vladimir I., Mikhail Sholukh, and Timo Korpela. "Use of protein–protein interactions in affinity chromatography." Journal of Biochemical and Biophysical Methods 49, no. 1-3 (October 2001): 29–47. http://dx.doi.org/10.1016/s0165-022x(01)00187-7.

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16

Hirano, Atsushi, Kentaro Shiraki, and Tomoshi Kameda. "Effects of Arginine on Multimodal Chromatography: Experiments and Simulations." Current Protein & Peptide Science 20, no. 1 (November 9, 2018): 40–48. http://dx.doi.org/10.2174/1389203718666171024115407.

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Multimodal or mixed-mode chromatography can be used to separate various proteins, including antibodies. The separation quality and efficiency have been improved by the addition of solutes, especially arginine. This review summarizes the mechanism underlying the effects of arginine on protein elution in multimodal chromatography with neutral, anionic or cationic resin ligands; the mechanism has been investigated using experiments and molecular dynamics simulations. Arginine is effective in facilitating protein elution compared to salts and protein denaturants such as guanidine and urea. The unique elution effect of arginine can be explained by the interplay among arginine, proteins and the resin ligands. Arginine exhibits multiple binding modes for the ligands and further affinity for protein aromatic residues through its guanidinium group. These properties make arginine versatile for protein elution in multimodal chromatography. Taking into account that arginine is an aggregation suppressor for proteins but not a protein denaturant, arginine is a promising protein-eluting reagent for multimodal chromatography.

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17

Chai, Pengdi, Xiuying Pu, Jianqiang Li, Xiaoyu Xia, Jun Ge, Amiao Luo, Hui Su, Weijie Zhang, and Jianzhong Ma. "Expression and Purification of Tetanus Toxin Fragment C in Escherichia coli BL21(DE3)." Protein & Peptide Letters 27, no. 11 (November 16, 2020): 1132–40. http://dx.doi.org/10.2174/0929866527666200528113327.

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Background: Tetanus is an infectious disease caused by Clostridium secreting tetanus toxin in anaerobic environment. The fragment C of Tetanus toxin (TTc) has been widely studied as a candidate vaccine to replace the existing tetanus toxoid vaccine. Objective: In this study, we established a simple method to purify recombinant protein TTc with ion-exchange chromatography from Escherichia coli expression systems. Methods: The TTc gene sequence was cloned into pET26b (+) vector and transferred to E. coli BL21 (DE3) for expression. The fermentation conditions (IPTG concentration, Induction temperature, Induction time) were optimized to obtain more soluble proteins. The soluble proteins were purified by Anion exchange chromatography and Cation exchange chromatography. The sequence of columns in the purification process was discussed. Finally, the stability of purified TTc protein were determined, the secondary structure of the purified TTc protein was determined by circular dichroism. The molecular weight of the purified TTc protein was determined by liquid chromatograph- mass spectrometer. Furthermore, we verified the immunogenicity of the purified protein in mice. Results: The purity of TTc improved from 34% to 88% after the first anion exchange column, and the final yield of recombinant TTc (purity > 95%) can reach 84.79% after the following cation exchange chromatography. The recombinant TTc had a molecular weight of 51.737 KDa, was stable at 4 °C and weak alkaline environment, was a β-sheet secondary structure, and had strong immunogenicity. Conclusion: The purification method we developed might be an efficient method for the industrial production of tetanus recombinant TTc vaccine.

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18

Winzor, D. J. "The development of chromatography for the characterization of protein interactions: a personal perspective." Biochemical Society Transactions 31, no. 5 (October 1, 2003): 1010–14. http://dx.doi.org/10.1042/bst0311010.

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This article reviews the progress of a personal endeavour to develop chromatography as a quantitative procedure for the determination of reaction stoichiometries and equilibrium constants governing protein interactions. As well as affording insight into an aspect of chromatography with which many protein chemists are unfamiliar, it shows the way in which minor adaptations of conventional chromatographic practices have rendered the technique one of the most powerful methods available for the characterization of interactions. That pathway towards quantification is followed from the introduction of frontal gel filtration for the study of protein self-association to the characterization of ligand binding by the biosensor variant of quantitative affinity chromatography.

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19

Keenan, M. J., and R. P. Holmes. "Chromatofocusing in the purification and separation of apo- and holo-(vitamin D-binding protein)." Biochemical Journal 229, no. 3 (August 1, 1985): 669–74. http://dx.doi.org/10.1042/bj2290669.

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Chromatofocusing was used to purify the vitamin D-binding protein (DBP) from pig plasma in a procedure that consisted of an initial DEAE-cellulose chromatography followed by DEAE-Sephadex chromatography, with final purification by chromatofocusing. The protein was purified 184-fold over its concentration in plasma. When the plasma was labelled with a tracer concentration of [3H]calcidiol, it was apparent that holo- and apo-DBP did not co-chromatograph on chromatofocusing. The separation of these two forms of DBP on chromatofocusing was verified by using purified apo-DBP mixed with either a tracer or a saturating concentration of calcidiol. This separation was consistent with differences observed in their isoelectric points. The ability to separate apo and holo forms of DBP should permit the study of their specific interactions with other binding proteins and help determine the physiological relevance of these interactions.

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20

Sikorski, M. M. "Expression of Lupinus luteus cDNA coding for PR10 protein in Escherichia coli: purification of the recombinant protein for structural and functional studies." Acta Biochimica Polonica 44, no. 3 (September 30, 1997): 565–78. http://dx.doi.org/10.18388/abp.1997_4405.

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The cDNA clones coding for two pathogenesis-related protein homologues of PR10 class, LlPR10.1A and LlPR10.1B, were identified in yellow lupin expression library of uninfected roots. The contribution of PR10 proteins to the overall mechanism of plant defence still remains unknown. In order to elucidate the structure and function of lupin PR10.1A protein, a substantial quantity of the protein was produced in an E. coli expression system using plasmids of pET-series: pET-3a and pET-15b, carrying the T7 promoter. Both plasmids with subcloned Llpr10.1a gene were overexpressed in E. coli, strain BL21(DE3)pLysS. The recombinant LlPR10.1A protein, overproduced in bacterial cells transformed with the pET-3a/Llpr10.1a plasmid, was purified to homogeneity from the insoluble "inclusion bodies" by ammonium sulphate fractionation and two sequential chromatographic steps: ion-exchange chromatography on DE 52 cellulose followed by size exclusion chromatography on Superdex 75 FPLC column. The (His)6 LlPR10.1A protein overproduced in E. coli cells harbouring the pET-15b/Llpr10.1a plasmid was purified by chromatography on Ni2+-charged His. Bind Resin. Western blot analysis with rabbit serum containing anti-LlPR10.1AN antibody revealed identical immunochemical properties of the two recombinant polypeptides and native LlPR10.1A protein. The recombinant protein produced in pET-3a plasmid was renatured from its insoluble form, concentrated up to 22 mg/ml and submitted to crystallisation. However, the LlPR10.1A protein expressed in pET-15b plasmid precipitated from the solution when at a higher concentration (10 mg/ml). This preparation was used at a lower concentration as an antigen for the preparation of polyclonal antibodies for immunochemical studies.

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21

Tanaka, Takuro, Koichiro Ikeda, Shuichi Yamamoto, and Noriko Yoshimoto. "Elution Profiles of Antibody-Drug Conjugates in Preparative Chromatography." MATEC Web of Conferences 333 (2021): 14001. http://dx.doi.org/10.1051/matecconf/202133314001.

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Monoclonal antibody drug conjugate (ADCs) have received much attention as pharmaceutical agents for treating serious diseases such as cancer. However, it is difficult to separate them on the basis of the drug to antibody ratio, DAR. Hydrophobic chromatography (HIC) is commonly used for the analysis of the drug to antibody ratio, DAR. The retention of ADCs on HIC can be controlled by the hydrophobic nature of ADCs, depending on the mobile phase conditions. They are sometimes performed at the restricted conditions where the solubility is too low. Ion exchange chromatography (IEC) using electrostatic interaction is an orthogonal method to HIC. IEC is widely used because of its higher capacity than HIC. We investigated the retention behavior of the protein conjugated with surrogate drugs on IEC. The surrogate drugs employed are 7-diethylamino-3-(4’-maleimidylhenyl) 4-methylcoumarin (CPM), N-(1-pyrenyl) maleimide (NPM). Bovine serum albumin (BSA) was used as a model protein. The molar ratio (CPM and NPM to protein) was set to 3. The maleimide group of CPM and NPM reacts with the thiol group of the proteins. On the linear gradient elution experiments, the elution salt concentrations of the conjugated and non-conjugated proteins were measured to obtain chromatographic parameter of the number of binding sites, B.

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22

Tanaka, Takuro, Koichiro Ikeda, Shuichi Yamamoto, and Noriko Yoshimoto. "Elution Profiles of Antibody-Drug Conjugates in Preparative Chromatography." MATEC Web of Conferences 333 (2021): 14001. http://dx.doi.org/10.1051/matecconf/202133314001.

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Monoclonal antibody drug conjugate (ADCs) have received much attention as pharmaceutical agents for treating serious diseases such as cancer. However, it is difficult to separate them on the basis of the drug to antibody ratio, DAR. Hydrophobic chromatography (HIC) is commonly used for the analysis of the drug to antibody ratio, DAR. The retention of ADCs on HIC can be controlled by the hydrophobic nature of ADCs, depending on the mobile phase conditions. They are sometimes performed at the restricted conditions where the solubility is too low. Ion exchange chromatography (IEC) using electrostatic interaction is an orthogonal method to HIC. IEC is widely used because of its higher capacity than HIC. We investigated the retention behavior of the protein conjugated with surrogate drugs on IEC. The surrogate drugs employed are 7-diethylamino-3-(4’-maleimidylhenyl) 4-methylcoumarin (CPM), N-(1-pyrenyl) maleimide (NPM). Bovine serum albumin (BSA) was used as a model protein. The molar ratio (CPM and NPM to protein) was set to 3. The maleimide group of CPM and NPM reacts with the thiol group of the proteins. On the linear gradient elution experiments, the elution salt concentrations of the conjugated and non-conjugated proteins were measured to obtain chromatographic parameter of the number of binding sites, B.

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23

Cooper, J. D. H., D. C. Turnell, B. Green, D. J. Wright, and E. J. Coombes. "Why the Assay of Serum Cystine by Protein Precipitation and Chromatography Should Be Abandoned." Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 25, no. 5 (September 1988): 577–82. http://dx.doi.org/10.1177/000456328802500516.

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The higher bias of serum cystine estimations by a HPLC method compared with those by ion exchange techniques is shown to be largely due to differences in the sample preparation procedures of the two techniques. The ion exchange methods utilised sulphosalicylic acid serum protein precipitation and post-column ninhydrin derivatisation of cystine, whilst the high pressure liquid chromatography technique employed automated dialysis for removal of proteins and pre-column ortho-phthalaldehyde derivatisation of cystine after its conversion to cysteine and then to S-carboxymethylcysteine. Examination of these procedures showed that whilst the high pressure liquid chromatographic method accurately estimates total serum cystine and cysteine, many factors affect the precision and accuracy of serum cystine estimations using the ion exchange techniques. In particular, serum protein precipitation techniques that are currently employed for the preparation of samples for cystine analysis by ion exchange chromatography should be abandoned.

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24

Arakawa, Tsutomu, and Yoshiko Kita. "Protein Solvent Interaction: Transition of Protein-solvent Interaction Concept from Basic Research into Solvent Manipulation of Chromatography." Current Protein & Peptide Science 20, no. 1 (November 9, 2018): 34–39. http://dx.doi.org/10.2174/1389203718666171024121529.

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Previously, we have reviewed in this journal (Arakawa, T., Kita, Y., Curr. Protein Pept. Sci., 15, 608-620, 2014) the interaction of arginine with proteins and various applications of this solvent additive in the area of protein formulations and downstream processes. In this special issue, we expand the concept of protein-solvent interaction into the analysis of the effects of solvent additives on various column chromatography, including mixed-mode chromatography. Earlier in our research, we have studied the interactions of such a variety of solvent additives as sugars, salts, amino acids, polymers and organic solvents with a variety of proteins, which resulted in mechanistic understanding on their protein stabilization and precipitation effects, the latter known as Hofmeister series. While such a study was then a pure academic research, rapid development of genetic engineering technologies and resultant biotechnologies made it a valuable knowledge in fully utilizing solvent additives in manipulation of protein solution, including column chromatography.

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25

TAKAHASHI, Sadao, Toshitaka TAMAI, Hirotada TAKAI, Shinta HAYASHI, Hajime MAEDA, Hiroyuki SAGE, Tsuguhiko INAKA, and Susumu MIYABO. "Lipoproteins Separation on Superose 6 Gel-Filtration Column Using Fast Protein Liquid Chromatography System." Journal of Japan Atherosclerosis Society 15, no. 5 (1987): 1179–83. http://dx.doi.org/10.5551/jat1973.15.5_1179.

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26

Bloustine, J., V. Berejnov, and S. Fraden. "Measurements of Protein-Protein Interactions by Size Exclusion Chromatography." Biophysical Journal 85, no. 4 (October 2003): 2619–23. http://dx.doi.org/10.1016/s0006-3495(03)74684-0.

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27

Soderstrom, M., R. Morgenstern, and S. Hammarstrom. "Protein-Protein Interaction Affinity Chromatography of Leukotriene C4 Synthase." Protein Expression and Purification 6, no. 3 (June 1995): 352–56. http://dx.doi.org/10.1006/prep.1995.1046.

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28

Tarrant, Richard D. R., M. Lourdes Velez-Suberbie, Andrew S. Tait, C. Mark Smales, and Daniel G. Bracewell. "Host cell protein adsorption characteristics during protein a chromatography." Biotechnology Progress 28, no. 4 (July 2012): 1037–44. http://dx.doi.org/10.1002/btpr.1581.

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29

Kumar, A., I. Yu Galaev, and B. Mattiasson. "Polymer displacement/shielding in protein chromatography." Journal of Chromatography B: Biomedical Sciences and Applications 741, no. 2 (May 2000): 103–13. http://dx.doi.org/10.1016/s0378-4347(00)00089-x.

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30

Leonard, M. "New packing materials for protein chromatography." Journal of Chromatography B: Biomedical Sciences and Applications 699, no. 1-2 (October 1997): 3–27. http://dx.doi.org/10.1016/s0378-4347(97)00160-6.

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31

Collins, William E. "Protein Separation with Flow-Through Chromatography." Separation and Purification Methods 26, no. 2 (January 1997): 215–53. http://dx.doi.org/10.1080/03602549708014159.

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32

Lightfoot, E. N., J. L. Coffman, Florian Lode, Q. S. Yuan, T. W. Perkins, and T. W. Root. "Refining the description of protein chromatography." Journal of Chromatography A 760, no. 1 (January 1997): 139–49. http://dx.doi.org/10.1016/s0021-9673(96)00843-6.

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33

McCue, Justin T., Glen Kemp, Duncan Low, and Igor Quiñones-Garcı́a. "Evaluation of protein-A chromatography media." Journal of Chromatography A 989, no. 1 (March 2003): 139–53. http://dx.doi.org/10.1016/s0021-9673(03)00005-0.

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34

Schlabach, Timothy D., and Kenneth J. Wilson. "Microbore flow-rates and protein chromatography." Journal of Chromatography A 385 (January 1987): 65–74. http://dx.doi.org/10.1016/s0021-9673(01)94622-9.

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35

Bereli, Nilay, Handan Yavuz, and Adil Denizli. "Protein chromatography by molecular imprinted cryogels." Journal of Liquid Chromatography & Related Technologies 43, no. 15-16 (July 21, 2020): 657–70. http://dx.doi.org/10.1080/10826076.2020.1780606.

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36

Ruckenstein, E., and V. Lesins. "Protein separation by potential barrier chromatography." Biotechnology and Bioengineering 28, no. 3 (March 1986): 432–51. http://dx.doi.org/10.1002/bit.260280317.

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37

Natarajan, Venkatesh, and Andrew L. Zydney. "Protein a chromatography at high titers." Biotechnology and Bioengineering 110, no. 9 (April 22, 2013): 2445–51. http://dx.doi.org/10.1002/bit.24902.

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38

Chang, Nancy, and Alexander M. Klibanov. "Protein chromatography in neat organic solvents." Biotechnology and Bioengineering 39, no. 5 (March 5, 1992): 575–78. http://dx.doi.org/10.1002/bit.260390513.

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39

Tateno, Hiroaki, Sachiko Nakamura-Tsuruta, and Jun Hirabayashi. "Frontal affinity chromatography: sugar–protein interactions." Nature Protocols 2, no. 10 (October 2007): 2529–37. http://dx.doi.org/10.1038/nprot.2007.357.

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40

Perret, Gérald, and Egisto Boschetti. "Aptamer affinity ligands in protein chromatography." Biochimie 145 (February 2018): 98–112. http://dx.doi.org/10.1016/j.biochi.2017.10.008.

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41

Sun, Yan. "Approaches to high-performance protein chromatography." Journal of Biotechnology 136 (October 2008): S288. http://dx.doi.org/10.1016/j.jbiotec.2008.07.619.

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42

Wetlaufer, D. B., and M. R. Koenigbauer. "Surfactant-mediated protein hydrophobic-interaction chromatography." Journal of Chromatography A 359 (January 1986): 55–60. http://dx.doi.org/10.1016/0021-9673(86)80061-9.

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43

Hober, Sophia, Karin Nord, and Martin Linhult. "Protein A chromatography for antibody purification." Journal of Chromatography B 848, no. 1 (March 2007): 40–47. http://dx.doi.org/10.1016/j.jchromb.2006.09.030.

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44

Mahn, Andrea, M. Elena Lienqueo, and Juan A. Asenjo. "A Simple Method for the Estimation of Protein Retention in Hydrophobic Interaction Chromatography Under Different Operation Conditions." Open Biotechnology Journal 1, no. 1 (May 25, 2007): 9–13. http://dx.doi.org/10.2174/1874070700701010009.

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Protein behavior in Hydrophobic Interaction Chromatography using different chromatographic conditions was investigated. A linear correlation was found between protein retention time on different matrixes and different initial elution salt concentrations. Mathematical correlations between retention times under different chromatographic conditions were obtained and validated, which can be used in process design and scale-up.

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45

Karkischenko, V. N., M. S. Dulya, D. V. Khvostov, R. A. Ageldinov, S. L. Lyublinskiy, and N. N. Karkischenko. "BIOLOGICALLY ACTIVE COMPONENTS OF ANTLERS EXTRACTS (CERVUS NIPPON) AND RED DEER (CERVUS ELAPHUS) PEPTIDEPROTEIN NATURE." Biomeditsina, no. 2 (July 1, 2019): 12–23. http://dx.doi.org/10.33647/2074-5982-15-2-12-23.

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A complex study of the protein composition of the biologically active components of the extracts of the velvet deer antlers (VDA, include Cervus nippon and Cervus elaphus) using two-dimensional gel electrophoresis (2D-PAGE), size-exclusion chromatography (SEC), and peptide mapping with high-performance liquid chromatography with mass spectrometric detection (HPLC-MS) with the use of fermentation by trypsin was done. A molecular-mass distribution characteristic for protein extracts of VDA has been established. Optimal conditions for extraction, chromatographic separation and relative quantitative determination of the main components have been determined. The results of the identification of the most significant (major and minor) protein components in the extracts of the studied objects are described in detail in accordance with the algorithm of the search program Spectrum Mill MS Proteomics Workbench and the protein database Uniprot. The data of protein profiling are clustered according to molecular and biological functions. The connections of the identified proteins with possible mechanisms of biological action and targets, which can be affected by the protein components of the studied objects, are presented. Based on the results of the study, conclusions about the multicomponent protein composition of extracts of VDA were drawn. The marker protein components in the studied extracts are suggested and the possible interrelationships of the detected proteins in the extracts with biological effects are indicated.

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46

Hirano, Atsushi, Tsutomu Arakawa, and Tomoshi Kameda. "3P049 Multimodal chromatography of proteins in arginine solutions(01C. Protein: Property,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))." Seibutsu Butsuri 54, supplement1-2 (2014): S257. http://dx.doi.org/10.2142/biophys.54.s257_1.

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Lesins, V., and E. Ruckenstein. "Protein Coated Adsorbents for use in Potential Barrier Chromatography: Fouling Chromatography." Biotechnology Progress 4, no. 1 (March 1988): 12–24. http://dx.doi.org/10.1002/btpr.5420040104.

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Peace, Robert W., and G. Sarwar Gilani. "Chromatographic Determination of Amino Acids in Foods." Journal of AOAC INTERNATIONAL 88, no. 3 (May 1, 2005): 877–87. http://dx.doi.org/10.1093/jaoac/88.3.877.

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Abstract Amino acids in foods exist in a free form or bound in peptides, proteins, or nonpeptide bonded polymers. Naturally occurring L-amino acids are required for protein synthesis and are precursors for essential molecules, such as co-enzymes and nucleic acids. Nonprotein amino acids may also occur in animal tissues as metabolic intermediates or have other important functions. The development of bacterially derived food proteins, genetically modified foods, and new methods of food processing; the production of amino acids for food fortification; and the introduction of new plant food sources have meant that protein amino acids and amino acid enantiomers in foods can have both nutritional and safety implications for humans. There is, therefore, a need for the rapid and accurate determination of amino acids in foods. Determination of the total amino acid content of foods requires protein hydrolysis by various means that must take into account variations in stability of individual amino acids and resistance of different peptide bonds to the hydrolysis procedures. Modern methods for separation and quantitation of free amino acids either before or after protein hydrolysis include ion exchange chromatography, high performance liquid chromatography (LC), gas chromatography, and capillary electrophoresis. Chemical derivatization of amino acids may be required to change them into forms amenable to separation by the various chromatographic methods or to create derivatives with properties, such as fluorescence, that improve their detection. Official methods for hydrolysis and analysis of amino acids in foods for nutritional purposes have been established. LC is currently the most widely used analytical technique, although there is a need for collaborative testing of methods available. Newer developments in chromatographic methodology and detector technology have reduced sample and reagent requirements and improved identification, resolution, and sensitivity of amino acid analyses of food samples.

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Fischer, Jenny J., Olivia Graebner, Mathias Dreger, Mirko Glinski, Sabine Baumgart, and Hubert Koester. "Improvement of Capture Compound Mass Spectrometry Technology (CCMS) for the Profiling of Human Kinases by Combination with 2D LC-MS/MS." Journal of Biomedicine and Biotechnology 2011 (2011): 1–5. http://dx.doi.org/10.1155/2011/850589.

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An increasingly popular and promising field in functional proteomics is the isolation of proteome subsets based on small molecule-protein interactions. One platform approach in this field are Capture Compounds that contain a small molecule of interest to bind target proteins, a photo-activatable reactivity function to covalently trap bound proteins, and a sorting function to isolate captured protein conjugates from complex biological samples for direct protein identification by liquid chromatography/mass spectrometry (nLC-MS/MS). In this study we used staurosporine as a selectivity group for analysis in HepG2 cells derived from human liver. In the present study, we combined the functional isolation of kinases with different separation workflows of automated split-free nanoflow liquid chromatography prior to mass spectrometric analysis. Two different CCMS setups, CCMS technology combined with 1D LC-MS and 2D LC-MS, were compared regarding the total number of kinase identifications. By extending the chromatographic separation of the tryptic digested captured proteins from 1D LC linear gradients to 2D LC we were able to identify 97 kinases. This result is similar to the 1D LC setup we previously reported but this time 4 times less input material was needed. This makes CCMS of kinases an even more powerful tool for the proteomic profiling of this important protein family.

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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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