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Journal articles on the topic 'Interferon Purification'

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Author: Grafiati

Published: 10 December 2022

Last updated: 29 January 2023

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1

Muttar, A. A. "Cloning and gene expression equine leukocyte α-interferon in cells of Escherichia Coli." Al-Qadisiyah Journal of Veterinary Medicine Sciences 12, no. 1 (June 30, 2013): 82. http://dx.doi.org/10.29079/vol12iss1art234.

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Interferon plays role in innate immune responses through upregulation of costimulatory molecules and induction of proinflammatory cytokines. interferons including interferon alpha (IFNA). The present study characterized IFNA cDNA and predicted protein. The interferon’s play a great role in protection from infections, which have been called by microorganisms, and also have powerful antiproliferation and immunomodulation activity. The purposes of study: cloning and expression of horse leukocyte interferon and purification the product protein. The results and discussion : In the result we isolated (DNA) from equine leukocyte in blood, which was used in the quality of the matrix for amplification of α-interferon gene with PCR HELP, and isolation gene α-interferon and transformation in vector puc18 and expression vector PET24b (+) and recombinant plasmid was transformed into E. coli strain BL21( codon plus 440) induction with IPTG. The results showed the protein having the same molecular weight as horse interferon alpha about 5.81 kDa

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2

Castro, Leonor S., Guilherme S. Lobo, Patrícia Pereira, Mara G. Freire, Márcia C. Neves, and Augusto Q. Pedro. "Interferon-Based Biopharmaceuticals: Overview on the Production, Purification, and Formulation." Vaccines 9, no. 4 (April 1, 2021): 328. http://dx.doi.org/10.3390/vaccines9040328.

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The advent of biopharmaceuticals in modern medicine brought enormous benefits to the treatment of numerous human diseases and improved the well-being of many people worldwide. First introduced in the market in the early 1980s, the number of approved biopharmaceutical products has been steadily increasing, with therapeutic proteins, antibodies, and their derivatives accounting for most of the generated revenues. The success of pharmaceutical biotechnology is closely linked with remarkable developments in DNA recombinant technology, which has enabled the production of proteins with high specificity. Among promising biopharmaceuticals are interferons, first described by Isaacs and Lindenmann in 1957 and approved for clinical use in humans nearly thirty years later. Interferons are secreted autocrine and paracrine proteins, which by regulating several biochemical pathways have a spectrum of clinical effectiveness against viral infections, malignant diseases, and multiple sclerosis. Given their relevance and sustained market share, this review provides an overview on the evolution of interferon manufacture, comprising their production, purification, and formulation stages. Remarkable developments achieved in the last decades are herein discussed in three main sections: (i) an upstream stage, including genetically engineered genes, vectors, and hosts, and optimization of culture conditions (culture media, induction temperature, type and concentration of inducer, induction regimens, and scale); (ii) a downstream stage, focusing on single- and multiple-step chromatography, and emerging alternatives (e.g., aqueous two-phase systems); and (iii) formulation and delivery, providing an overview of improved bioactivities and extended half-lives and targeted delivery to the site of action. This review ends with an outlook and foreseeable prospects for underdeveloped aspects of biopharma research involving human interferons.

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3

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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4

ADOLF, GÜNTHER R., ELISABETH TRAXLER, and INGRID MAURER-FOGY. "Recombinant Equine Interferon-β1: Purification and Preliminary Characterization." Journal of Interferon Research 10, no. 3 (June 1990): 255–67. http://dx.doi.org/10.1089/jir.1990.10.255.

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5

MATSUDA, SUSUMU, JUN UTSUMI, and GENJI KAWANO. "Purification and Characterization of Recombinant Mouse Interferon-β." Journal of Interferon Research 6, no. 5 (October 1986): 519–26. http://dx.doi.org/10.1089/jir.1986.6.519.

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6

Nagata, Kiyoshi, Norihisa Kikuchi, Osamu Ohara, Hiroshi Teraoka, Nobuo Yoshida, and Yoshimi Kawade. "Purification and characterization of recombinant murine immune interferon." FEBS Letters 205, no. 2 (September 15, 1986): 200–204. http://dx.doi.org/10.1016/0014-5793(86)80897-3.

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7

WILSON, MARK J., ROBERT B. FREEDMAN, and JOHN E. FITTON. "Recovery, refolding and purification of recombinant α2-interferon." Biochemical Society Transactions 16, no. 1 (February 1, 1988): 58–59. http://dx.doi.org/10.1042/bst0160058a.

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8

Olsson, Tomas, Moiz Bakhiet, Bo Höjeberg, Åke Ljungdahl, Sofija Kelic, Conny Edlund, Krister Kristensson, and Peter H. Van Der Meide. "Neuronal interferon-γ immunoreactive molecule: Bioactivities and purification." European Journal of Immunology 24, no. 2 (February 1994): 308–14. http://dx.doi.org/10.1002/eji.1830240205.

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9

Abolhassani, Mohsen, and Karen L. Jacobsen. "Purification of an acid-stable bovine leukocyte interferon." Veterinary Immunology and Immunopathology 29, no. 1-2 (August 1991): 171–81. http://dx.doi.org/10.1016/0165-2427(91)90062-h.

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10

Fountoulakis, M., E. Takacsdilorenzo, J. F. Juranville, and M. Manneberg. "Purification of Interferon γ-Interferon γ Receptor Complexes by Preparative Electrophoresis on Native Gels." Analytical Biochemistry 208, no. 2 (February 1993): 270–76. http://dx.doi.org/10.1006/abio.1993.1045.

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11

Badiee Kheirabadi, Seyedeh Elham, Kazem Mashayekhi, Malihe Moghadam, Mohammad Javad Mousavi, and Mojtaba Sankian. "Cloning, Expression, and Purification of Recombinant Mouse Interferon-γ." Research in Molecular Medicine 9, no. 1 (January 25, 2021): 1–10. http://dx.doi.org/10.32598/rmm.9.1.1.

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Background: Interferon-gamma [IFN-γ) is the most important cytokine in the immune system. This protein has been expressed in bacterial cells. However, bacterial cloning is not an easy task. We aimed to clone, express, and purify recombinant mouse IFN-γ and overcome problems in favor of commercial purposes. Materials and Methods: To amplify the gene product for cloning, we primarily designed two specific primers for the target gene. Following PCR amplification, the amplicon was inserted into the pET-21b[+) vector. The E. coli BL21 [DE3) CodonPlus strain was chosen for the expression of the target gene. Finally, the expressed recombinant mouse IFN-γ was assessed through the western blotting method. Results: We performed a cloning process and produced recombinant mouse IFN-γ in an optimal condition. We also noticed that monomeric protein could be transformed to a homodimeric structure which can be observed using the SDS PAGE [SDS-polyacrylamide gel electrophoresis) and western blotting. Conclusion: Experimental conditions strongly affect the large-scale cloning procedures required to be optimized in each laboratory. The expressed recombinant mouse IFN-γ described here is appropriate for commercial purposes.

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12

CIVAS, AHMET, Bernard FOURNET, Colette COULOMBEL, Daniele ROSCOUET, Anne HONVAULT, Fahrettin PETEK, Jean MONTREUIL, and Janine DOLY. "Purification and carbohydrate structure of natural murine interferon-beta." European Journal of Biochemistry 173, no. 2 (April 1988): 311–16. http://dx.doi.org/10.1111/j.1432-1033.1988.tb14000.x.

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13

Yasuda, Masayukl, Robert A. Good, and Noorbibl K. Day. "Partial Purification and Characterization of Feline Gamma-Like Interferon." Preparative Biochemistry 16, no. 3 (September 1986): 217–26. http://dx.doi.org/10.1080/00327488608062467.

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14

Zhang, Z., K. T. Tong, M. Belew, T. Pettersson, and J. C. Janson. "Production, purification and characterization of recombinant human interferon γ." Journal of Chromatography A 604, no. 1 (June 1992): 143–55. http://dx.doi.org/10.1016/0021-9673(92)85539-6.

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15

Kohase, M., H. Moriya, T. A. Sato, S. Kohno, and S. Yamazaki. "Purification and Characterization of Chick Interferon Induced by Viruses." Journal of General Virology 67, no. 1 (January 1, 1986): 215–18. http://dx.doi.org/10.1099/0022-1317-67-1-215.

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16

Li, Mingcai, and Dongyang Huang. "Purification and characterization of prokaryotically expressed human interferon-λ2." Biotechnology Letters 29, no. 7 (March 31, 2007): 1025–29. http://dx.doi.org/10.1007/s10529-007-9357-y.

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17

Notani, Joji, Tsutomu Kaizu, Seitarou Mutoh, Kazuyuki Otsuka, Chihiro Kusunoki, Hisashi Yamada, Akira Nagayoshi, et al. "Application of Namalva Interferon-α Monoclonal Antibodies for Purification and Enzyme Immnoassay of Interferon-α." Journal of Immunoassay 10, no. 2-3 (June 1989): 257–76. http://dx.doi.org/10.1080/01971528908053240.

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18

GRIBAUDO, GIORGIO, FRANCA COFANO, MARIA PRAT, and SANTO LANDOLFO. "Monoclonal Antibodies to Murine Interferon-γ: Affinity Purification and Molecular Characterization of Murine Interferon-γ." Journal of Interferon Research 5, no. 1 (January 1985): 199–208. http://dx.doi.org/10.1089/jir.1985.5.199.

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19

Peng, Fu-Wang, Zhao-Jun Duan, Li-Shu Zheng, Zhi-Ping Xie, Han-Chun Gao, Hui Zhang, Wu-Ping Li, and Yun-De Hou. "Purification of recombinant human interferon-ε and oligonucleotide microarray analysis of interferon-ε-regulated genes." Protein Expression and Purification 53, no. 2 (June 2007): 356–62. http://dx.doi.org/10.1016/j.pep.2006.12.013.

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20

Dembinski, W. E., and E. Sulkowski. "Improved Large Scale Purification Procedure of Natural Human Fibroblast Interferon." Preparative Biochemistry 16, no. 2 (June 1986): 175–86. http://dx.doi.org/10.1080/10826068608062278.

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21

Houard, Sophie, Alain Jacquet, Michèle Haumont, Florence Glineur, Véronique Daminet, Fabienne Milican, and Alex Bollen. "Cloning, expression and purification of recombinant cotton rat interferon-gamma." Gene 240, no. 1 (November 1999): 107–13. http://dx.doi.org/10.1016/s0378-1119(99)00424-2.

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22

Scapol, L., P. Rappuoli, and G. C. Viscomi. "Purification of recombinant human interferon-β by immobilized antisense peptides." Journal of Chromatography A 600, no. 2 (May 1992): 235–42. http://dx.doi.org/10.1016/0021-9673(92)85553-6.

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23

Windsor, William T., Leigh J. Walter, Rosalinda Syto, James Fossetta, William J. Cook, Tattanahalli L. Nagabhushan, and Mark R. Walter. "Purification and crystallization of a complex between human interferon γ receptor (extracellular domain) and human interferon γ." Proteins: Structure, Function, and Genetics 26, no. 1 (September 1996): 108–14. http://dx.doi.org/10.1002/(sici)1097-0134(199609)26:1<108::aid-prot10>3.0.co;2-k.

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24

WANG, DAN, HUI REN, JING-WEI XU, PENG-DA SUN, and XUE-DONG FANG. "Expression, purification and characterization of human interferon-γ in Pichia pastoris." Molecular Medicine Reports 9, no. 2 (November 19, 2013): 715–19. http://dx.doi.org/10.3892/mmr.2013.1812.

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25

Novick, D., P. Orchansky, M. Revel, and M. Rubinstein. "The human interferon-gamma receptor. Purification, characterization, and preparation of antibodies." Journal of Biological Chemistry 262, no. 18 (June 1987): 8483–87. http://dx.doi.org/10.1016/s0021-9258(18)47439-x.

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26

Srivastava, Poonam, Palash Bhattacharaya, Gaurav Pandey, and K. J. Mukherjee. "Overexpression and purification of recombinant human interferon alpha2b in Escherichia coli." Protein Expression and Purification 41, no. 2 (June 2005): 313–22. http://dx.doi.org/10.1016/j.pep.2004.12.018.

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27

Calderon, J., K. C. Sheehan, C. Chance, M. L. Thomas, and R. D. Schreiber. "Purification and characterization of the human interferon-gamma receptor from placenta." Proceedings of the National Academy of Sciences 85, no. 13 (July 1, 1988): 4837–41. http://dx.doi.org/10.1073/pnas.85.13.4837.

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28

Swaminathan, Sathyamangalam, and Navin Khanna. "Affinity Purification of Recombinant Interferon-α on a Mimetic Ligand Adsorbent." Protein Expression and Purification 15, no. 2 (March 1999): 236–42. http://dx.doi.org/10.1006/prep.1998.1017.

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29

Zoon, K. C., D. Miller, J. Bekisz, D. zur Nedden, J. C. Enterline, N. Y. Nguyen, and R. Q. Hu. "Purification and characterization of multiple components of human lymphoblastoid interferon-alpha." Journal of Biological Chemistry 267, no. 21 (July 1992): 15210–16. http://dx.doi.org/10.1016/s0021-9258(18)42167-9.

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30

Prakash, Krishna, and Pramod C. Rath. "Mouse interferon regulatory factor-2: expression, purification and DNA binding activity." Molecular Biology Reports 39, no. 1 (May 11, 2011): 599–606. http://dx.doi.org/10.1007/s11033-011-0776-4.

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31

Tsukui, Kazuo, Shigeharu Uchida, Eiichi Tokunaga, and Yoshimi Kawade. "A Monoclonal Antibody with Broad Reactivity to Human Interferon-α Subtypes Useful for Purification of Leukocyte-Derived Interferon." Microbiology and Immunology 30, no. 11 (November 1986): 1129–39. http://dx.doi.org/10.1111/j.1348-0421.1986.tb03042.x.

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32

Harris, Bethany D., Jessica Schreiter, Marc Chevrier, Jarrat L. Jordan, and Mark R. Walter. "Human interferon-ϵ and interferon-κ exhibit low potency and low affinity for cell-surface IFNAR and the poxvirus antagonist B18R." Journal of Biological Chemistry 293, no. 41 (August 31, 2018): 16057–68. http://dx.doi.org/10.1074/jbc.ra118.003617.

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IFNϵ and IFNκ are interferons that induce microbial immunity at mucosal surfaces and in the skin. They are members of the type-I interferon (IFN) family, which consists of 16 different IFNs, that all signal through the common IFNAR1/IFNAR2 receptor complex. Although IFNϵ and IFNκ have unique expression and functional properties, their biophysical properties have not been extensively studied. In this report, we describe the expression, purification, and characterization of recombinant human IFNϵ and IFNκ. In cellular assays, IFNϵ and IFNκ exhibit ∼1000-fold lower potency than IFNα2 and IFNω. The reduced potency of IFNϵ and IFNκ are consistent with their weak affinity for the IFNAR2 receptor chain. Despite reduced IFNAR2-binding affinities, IFNϵ and IFNκ exhibit affinities for the IFNAR1 chain that are similar to other IFN subtypes. As observed for cellular IFNAR2 receptor, the poxvirus antagonist, B18R, also exhibits reduced affinity for IFNϵ and IFNκ, relative to the other IFNs. Taken together, our data suggest IFNϵ and IFNκ are specialized IFNs that have evolved to weakly bind to the IFNAR2 chain, which allows innate protection of the mucosa and skin and limits neutralization of IFNϵ and IFNκ biological activities by viral IFN antagonists.

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33

Tyurin, Alexander A., Orkhan Mustafaev, Aleksandra V. Suhorukova, Olga S. Pavlenko, Viktoriia A. Fridman, Ilya S. Demyanchuk, and Irina V. Goldenkova-Pavlova. "Modulation of the Translation Efficiency of Heterologous mRNA and Target Protein Stability in a Plant System: The Case Study of Interferon-αA." Plants 11, no. 19 (September 20, 2022): 2450. http://dx.doi.org/10.3390/plants11192450.

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A broad and amazingly intricate network of mechanisms underlying the decoding of a plant genome into the proteome forces the researcher to design new strategies to enhance both the accumulation of recombinant proteins and their purification from plants and to improve the available relevant strategies. In this paper, we propose new approaches to optimize a codon composition of target genes (case study of interferon-αA) and to search for regulatory sequences (case study of 5′UTR), and we demonstrated their effectiveness in increasing the synthesis of recombinant proteins in plant systems. In addition, we convincingly show that the approach utilizing stabilization of the protein product according to the N-end rule or a new protein-stabilizing partner (thermostable lichenase) is sufficiently effective and results in a significant increase in the protein yield manufactured in a plant system. Moreover, it is validly demonstrated that thermostable lichenase as a protein-stabilizing partner not only has no negative effect on the target protein activity (interferon-αA) integrated in its sequence, but rather enhances the accumulation of the target protein product in plant cells. In addition, the retention of lichenase enzyme activity and interferon biological activity after the incubation of plant protein lysates at 65 °C and precipitation of nontarget proteins with ethanol is applicable to a rapid and inexpensive purification of fusion proteins, thereby confirming the utility of thermostable lichenase as a protein-stabilizing partner for plant systems.

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34

Salunkhe, Shardul, Bhaskarjyoti Prasad, Ketaki Sabnis-Prasad, Anjali Apte-Deshpande, and Sriram Padmanabhan. "Expression and Purification of SAK-fused Human Interferon Alpha in Escherichia coli." Journal of Microbial & Biochemical Technology 01, no. 01 (2009): 005–10. http://dx.doi.org/10.4172/1948-5948.1000002.

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35

Hughes, T. K., E. M. Smith, and J. E. Blalock. "Interferon Inducing Transformed Cell Surface Glycoproteins: Purification by Ia Antigen Affinity Chromatography." Experimental Biology and Medicine 182, no. 4 (September 1, 1986): 564–67. http://dx.doi.org/10.3181/00379727-182-4-rc2.

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36

Cai, Meihong, Feng Zhu, and Pingping Shen. "Expression and purification of chicken beta interferon and its antivirus immunological activity." Protein Expression and Purification 84, no. 1 (July 2012): 123–29. http://dx.doi.org/10.1016/j.pep.2012.04.014.

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37

Geng, Xindu, Quan Bai, Yangjun Zhang, Xiang Li, and Dan Wu. "Refolding and purification of interferon-gamma in industry by hydrophobic interaction chromatography." Journal of Biotechnology 113, no. 1-3 (September 2004): 137–49. http://dx.doi.org/10.1016/j.jbiotec.2004.06.006.

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38

Basu, M., J. L. Pace, D. M. Pinson, M. P. Hayes, P. P. Trotta, and S. W. Russell. "Purification and partial characterization of a receptor protein for mouse interferon gamma." Proceedings of the National Academy of Sciences 85, no. 17 (September 1, 1988): 6282–86. http://dx.doi.org/10.1073/pnas.85.17.6282.

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39

Moellering, Bill J., Steven K. Yoshinaga, Ariela Hui, John M. Delaney, Shinichi Hara, Linda O. Narhi, and Keith R. Westcott. "Folding and Purification of a Recombinantly Expressed Interferon Regulatory Factor, IRF-4." Protein Expression and Purification 16, no. 1 (June 1999): 160–70. http://dx.doi.org/10.1006/prep.1999.1065.

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40

Lai, Chun-Yen, Elizabeth Dharm, and Yutaka Fujii. "Purification and structural characterization of recombinant rat γ-interferon from Escherichia coli." Analytical Biochemistry 176, no. 2 (February 1989): 326–29. http://dx.doi.org/10.1016/0003-2697(89)90317-5.

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41

Aguet, M., and G. Merlin. "Purification of human gamma interferon receptors by sequential affinity chromatography on immobilized monoclonal antireceptor antibodies and human gamma interferon." Journal of Experimental Medicine 165, no. 4 (April 1, 1987): 988–99. http://dx.doi.org/10.1084/jem.165.4.988.

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mAbs against human IFN-gamma (huIFN-gamma) receptors were obtained by immunizing a BALB/c mouse with eluates from immobilized recombinant huIFN-gamma (rhuIFN-gamma) on which lysates of enriched Raji cell membranes had been adsorbed. mAbs were selected for competitive inhibition of receptor binding of 125I-labeled rhuIFN-gamma. The following additional properties suggest that these antibodies are specific for huIFN-gamma receptors: they bind to the surface of human cells expressing IFN-gamma receptors but not to heterologous cells; this binding is inhibited competitively by addition of rhuIFN-gamma; the number of binding sites revealed by direct binding of 125I-labeled rhuIFN-gamma correlates with the amount of antigen recognized by the mAbs on different cell lines. A Triton X-100 extract of a membrane-enriched fraction of human Raji cells was affinity purified with these mAbs and the eluates from such columns were further purified on immobilized rhuIFN-gamma. As revealed by SDS-PAGE, the final eluate contained two major protein bands with approximate Mr of 90,000 (p90) and 50,000 (p50), respectively. Both proteins were able to specifically bind 125I-labeled rhuIFN-gamma upon electroblotting to nitrocellulose. This binding could be inhibited by the huIFN-gamma receptor mAbs, suggesting that the same epitopes are recognized on p90, p50, and on the cell surface. Therefore, these proteins most likely represent at least a part of huIFN-gamma receptors.

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42

Doğan, Ali, Serpil Özkara, Müfrettin Murat Sarı, Lokman Uzun, and Adil Denizli. "Evaluation of human interferon adsorption performance of Cibacron Blue F3GA attached cryogels and interferon purification by using FPLC system." Journal of Chromatography B 893-894 (April 2012): 69–76. http://dx.doi.org/10.1016/j.jchromb.2012.02.036.

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43

Saugandhika, Shrabani, Vishal Sharma, Hrudananda Malik, Sikander Saini, Sudam Bag, Sudarshan Kumar, Niraj Kumar Singh, Ashok Kumar Mohanty, and Dhruba Malakar. "Expression and purification of buffalo interferon-tau and efficacy of recombinant buffalo interferon-tau for in vitro embryo development." Cytokine 75, no. 1 (September 2015): 186–96. http://dx.doi.org/10.1016/j.cyto.2015.03.012.

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44

Bazer, Fuller W., and William W. Thatcher. "Chronicling the discovery of interferon tau." Reproduction 154, no. 5 (November 2017): F11—F20. http://dx.doi.org/10.1530/rep-17-0257.

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It has been 38 years since a protein, now known as interferon tau (IFNT), was discovered in ovine conceptus-conditioned culture medium. After 1979, purification and testing of native IFNT revealed its unique antiluteolyic activity to prevent the regression of corpora lutea on ovaries of nonpregnant ewes. Antiviral, antiproliferative and immunomodulatory properties of native and recombinant IFNT were demonstrated later. In addition, progesterone and IFNT were found to act cooperatively to silence expression of classical interferon stimulated genes in a cell-specific manner in ovine uterine luminal and superficial glandular epithelia. But, IFNT signaling through a STAT1/STAT2-independent pathway stimulates expression of genes, such as those for transport of glucose and amino acids, which are required for growth and development of the conceptus. Further, undefined mechanisms of action of IFNT are key to a servomechanism that allows ovine placental lactogen and placental growth hormone to affect the development of uterine glands and their expression of genes throughout gestation. IFNT also acts systemically to induce the expression of interferon stimulated genes that influence secretion of progesterone by the corpus luteum. Finally, IFNT has great potential as a therapeutic agent due to its low cytotoxicity, anti-inflammatory properties and effects to mitigate diabetes, obesity-associated syndromes and various autoimmune diseases.

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45

Rehemtulla, A., P. Murphy, M. Dobson, and D. A. Hart. "Purification and partial characterization of a plasminogen activator inhibitor from the human glioblastoma, U138." Biochemistry and Cell Biology 66, no. 12 (December 1, 1988): 1270–77. http://dx.doi.org/10.1139/o88-147.

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A plasminogen activator inhibitor was purified to apparent homogeneity from conditioned media of U138 cells. The inhibitor is a glycoprotein with a pI of 5.4 and an apparent molecular weight of 45 000. The inhibitor forms sodium dodecyl sulfate-stable complexes with plasminogen activators and trypsin but not with plasmin, thrombin, or pancreatic kallikrein. Some biochemical and immunochemical characteristics of the U138 inhibitor distinguish it from other known plasminogen activator inhibitors. The expression of this inhibitor by U138 cells could be modulated by incubation in phorbol myristate acetate, interleukin-1, tumor necrosis factor, and γ interferon, but not in β interferon. Thus, the expression of the plasminogen activator inhibitor can be influenced by biological response modifiers known to be active in the brain and in the neural response to inflammatory stimuli. Therefore, this inhibitor, along with protease nexin, may be involved in brain development and regulation.

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46

Pine, R., T. Decker, D. S. Kessler, D. E. Levy, and J. E. Darnell. "Purification and cloning of interferon-stimulated gene factor 2 (ISGF2): ISGF2 (IRF-1) can bind to the promoters of both beta interferon- and interferon-stimulated genes but is not a primary transcriptional activator of either." Molecular and Cellular Biology 10, no. 6 (June 1990): 2448–57. http://dx.doi.org/10.1128/mcb.10.6.2448-2457.1990.

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Interferon-stimulated gene factor 2 (ISGF2) was purified from HeLa cells treated with alpha interferon. The factor, a single polypeptide of 56 kilodaltons (kDa), bound both to the central 9 base pairs of the 15-base-pair interferon-stimulated response element (ISRE) that is required for transcriptional activation of interferon-stimulated genes and to the PRD-I regulatory element of the beta interferon gene. ISGF2 was a phosphoprotein, and dephosphorylation in vitro reduced its DNA-binding activity. However, conditions that changed the amount of ISGF2 did not change the phosphorylated isoforms in vivo. ISGF2 in unstimulated cells existed in trace amounts and was induced by both alpha interferon and gamma interferon as well as by virus infection. Plasmid-bearing Escherichia coli clones encoding ISGF2 were selected with antibody against purified ISGF2. Sequence analysis revealed that the ISGF2 protein was the same as that encoded by the cDNA clone IRF-1, which has been claimed to activate transcription of interferon genes. We show that transcription of the ISGF2 gene was induced by alpha interferon, gamma interferon, and double-stranded RNA. However, ISGF2 was neither necessary nor sufficient for induced transcription of the beta interferon gene, while the factor NF kappa B was clearly involved.

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47

Pine, R., T. Decker, D. S. Kessler, D. E. Levy, and J. E. Darnell. "Purification and cloning of interferon-stimulated gene factor 2 (ISGF2): ISGF2 (IRF-1) can bind to the promoters of both beta interferon- and interferon-stimulated genes but is not a primary transcriptional activator of either." Molecular and Cellular Biology 10, no. 6 (June 1990): 2448–57. http://dx.doi.org/10.1128/mcb.10.6.2448.

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Abstract:

Interferon-stimulated gene factor 2 (ISGF2) was purified from HeLa cells treated with alpha interferon. The factor, a single polypeptide of 56 kilodaltons (kDa), bound both to the central 9 base pairs of the 15-base-pair interferon-stimulated response element (ISRE) that is required for transcriptional activation of interferon-stimulated genes and to the PRD-I regulatory element of the beta interferon gene. ISGF2 was a phosphoprotein, and dephosphorylation in vitro reduced its DNA-binding activity. However, conditions that changed the amount of ISGF2 did not change the phosphorylated isoforms in vivo. ISGF2 in unstimulated cells existed in trace amounts and was induced by both alpha interferon and gamma interferon as well as by virus infection. Plasmid-bearing Escherichia coli clones encoding ISGF2 were selected with antibody against purified ISGF2. Sequence analysis revealed that the ISGF2 protein was the same as that encoded by the cDNA clone IRF-1, which has been claimed to activate transcription of interferon genes. We show that transcription of the ISGF2 gene was induced by alpha interferon, gamma interferon, and double-stranded RNA. However, ISGF2 was neither necessary nor sufficient for induced transcription of the beta interferon gene, while the factor NF kappa B was clearly involved.

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Cheng, Y. S., M. F. Becker-Manley, T. P. Chow, and D. C. Horan. "Affinity purification of an interferon-induced human guanylate-binding protein and its characterization." Journal of Biological Chemistry 260, no. 29 (December 1985): 15834–39. http://dx.doi.org/10.1016/s0021-9258(17)36334-2.

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Beldarraín, Alejandro, Yai Cruz, Oscar Cruz, Monica Navarro, and Miriela Gil. "Purification and conformational properties of a human interferon α2b produced in Escherichia coli." Biotechnology and Applied Biochemistry 33, no. 3 (June 1, 2001): 173. http://dx.doi.org/10.1042/ba20010001.

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HAVELL, EDWARD A. "Purification and Further Characterization of an Anti-Murine Interferon-γ Monoclonal Neutralizing Antibody." Journal of Interferon Research 6, no. 5 (October 1986): 489–97. http://dx.doi.org/10.1089/jir.1986.6.489.

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