Relevant bibliographies by topics / Interferon Purification

Academic literature on the topic 'Interferon Purification'

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Published: 10 December 2022
Last updated: 29 January 2023

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Journal articles on the topic "Interferon Purification"

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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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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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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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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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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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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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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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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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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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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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Dissertations / Theses on the topic "Interferon Purification"

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Brooks, Paul. "Subcellular localization, induction by #gamma#-interferon and purification of the proteasome activator PA28." Thesis, University of Bristol, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.324332.

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Antunes, Joana Raquel Amaral. "Production and purification of interferon alpha-2b from Escherichia coli cultures using alternative platforms." Master's thesis, Universidade de Aveiro, 2017. http://hdl.handle.net/10773/22542.

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Mestrado em Biotecnologia - Biotecnologia Industrial e Ambiental
A indústria biofarmacêutica tem vindo a desenvolver diferentes tipos de biofármacos para o tratamento de diversas doenças. A maioria das proteínas terapêuticas são produzidas através da tecnologia do DNA recombinante, e purificadas utilizando técnicas convencionais, tais como a precipitação com sais, eletroforese e cromatografia. O interferão alfa-2b (IFNα-2b) é uma proteína terapêutica de ação imunomoduladora com atividade antiviral e antiproliferativa, que é geralmente obtida a partir de culturas de Escherichia coli, e utilizada no tratamento de doenças humanas, tais como a hepatite C, melanomas, alguns linfomas e leucemias, entre outras. Embora a fase de produção recombinante do IFNα-2b já tenha sido amplamente estudada e otimizada, a sua recuperação e purificação assumem-se como os passos economicamente limitantes do processo global de produção. Neste estudo, o IFNα-2b foi produzido na forma de corpos de inclusão utilizando culturas de BL21, no meio SOB, após 3 h de indução. A recuperação desta fração englobou vários passos, tendo sido alcançado um protocolo final que inclui: 1) Lavagem com Triton-X a 1%; 2) Lavagem com ureia a 4 M; e 3) Solubilização em meio alcalino, com ureia a 8 M. Alterando as condições de produção conseguiu-se também produzir e recuperar parte da proteína alvo na forma solúvel, embora com menor rendimento. O IFNα-2b previamente solubilizado foi purificado através de cromatografia aniónica, tendo sido obtido na sua forma biologicamente ativa com uma pureza superior a 95%. Como técnica alternativa de purificação utilizaram-se sistemas aquosos bifásicos constituídos por vários líquidos iónicos e tampão fosfato. Apesar de os resultados serem menos promissores, este estudo permitiu estudar plataformas alternativas para a recuperação e purificação do IFNα-2b através da aplicação de sistemas aquosos bifásicos.
The biopharmaceutical industry has been developing various biopharmaceutical possibilities for the treatment of several diseases. Most therapeutic proteins are produced through the recombinant protein technology and purified using traditional techniques, such as precipitation with salts, electrophoresis and chromatography. Interferon alfa-2b (IFNα-2b) is a therapeutic protein with immunomodulatory action and antiviral and antiproliferative activities, usually produced by Escherichia coli cultures, and used in the treatment of several human diseases, such as hepatitis C, melanomas, some lymphomas and leukemias, among others. Although the recombinant production of IFNα-2b has already been extensively studied and optimized, its recovery and purification correspond to the economically limiting steps of the overall production process. In this study, IFNα-2b was produced in the form of inclusion bodies using BL21 cultures, in SOB medium, after 3 h of induction. The recovery of this fraction involved several steps, and a final protocol was developed: 1) Washing with Triton-X at 1%; 2) Washing with urea at 4 M; and 3) Solubilization in alkaline medium with urea at 8 M. By changing the production conditions, it was also possible to produce and recover part of the target protein in the soluble form, yet with a lower yield. The solubilized IFNα-2b was purified using anion-exchange chromatography, and obtained in a biologically active form with a purity higher than 95 %. As an alternative purification technique, aqueous two-phase systems composed of several ionic liquids and a phosphate buffer were investigated. Although the results obtained are less promising, this study allowed the evaluation of alternative platforms for the recovery and purification of IFNα-2b by the application of aqueous two-phase systems.
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Dias, Paulo Victor Sarmento. "Desenvolvimento de processo de produção e caracterização de interferon-α2a secretado no espaço periplásmico de Escherichia Coli." Universidade de São Paulo, 2017. http://www.teses.usp.br/teses/disponiveis/85/85131/tde-04122017-150200/.

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Os IFN-α2 são atualmente utilizados em terapia de hepatite B e C, leucemia, mieloma múltiplo, leucemia de células pilosas, melanoma, sarcoma de Kaposi, linfoma folicular e carcinoma de células renais, em associação ou não com outras drogas. Este trabalho descreve um processo de produção, purificação e caracterização de interferon-α2a secretado para o espaço periplasmico de E. coli utilizando um vetor baseado no uso constitutivo do promotor lambda PL. Foi validada também uma análise em cromatografia líquida de alta eficiência em fase reversa (RP-HPLC) para monitoração do processo. Dessa forma, este trabalho descreve inicialmente um método de RP-HPLC para análise qualitativa e quantitativa de interferon-α2a e interferon-α2b. O método foi desenvolvido e validado quanto à recuperação, precisão, linearidade, sensibilidade e especificidade. O teste de recuperação indicou erro menor que 1 % e as determinações quantitativas intra-dia e inter-dia apresentaram desvio padrão relativo sempre menores que 4 %, enquanto a sensibilidade experimental foi de 0,3 μg (RSD = 5 %). Em relação à linearidade, o coeficiente de correlação assumiu o valor de 0,998 (p<0,0001), para o intervalo de massa analisada de 0,62 a 10 μg de interferon. Essa metodologia permite a aplicação de RP-HPLC como uma ferramenta poderosa para monitoração de níveis de expressão e qualidade do interferon-α2 durante ou logo após a fermentação. A temperatura ótima de expressão foi avaliada nos intervalos de 30 a 42 °C, em cultivo em erlenmeyer. As produções volumétrica e específica foram maiores para temperaturas iguais ou superiores a 35 °C. Dessa forma, considerando a potencial degradação da proteína recombinante induzida pela temperatura, a temperatura ótima para a expressão de interferon neste processo foi definida como 35 °C. Os maiores valores de produção específica e volumétrica obtidos, em produção em erlenmeyer, foram 1,04 μg/mL/A600 e 3,45 mg/L, respectivamente. Foi padronizado um método de purificação laboratorial, em duas etapas: uma cromatografia de troca iônica, seguida de uma etapa de cromatografia de exclusão molecular. A pureza final e a recuperação em massa foram de, respectivamente, 95,3 % e 66 %. O produto final também foi caracterizado por meio de análise em SDS-PAGE, western blotting, espectrometria de massas, HPLC de exclusão molecular e HPLC em fase reversa.
IFN-α2 is currently utilized in hepatitis B and C, leukemia, multiple myeloma, hairy cell leukemia, melanoma, Kaposi\'s sarcoma, follicular lymphoma, and renal cell carcinoma therapy, with or without other drugs. In this work, a process for E. coli periplasmic interferon-α2a production and purification utilizing a lambda PL promoter based on constitutive expression was proposed. As a tool for production monitoring, reversedphase high-performance liquid chromatography (RP-HPLC) analysis directly from periplasmic extract was validated. Thus, initially it was described a RP-HPLC methodology for qualitative and quantitative analysis of recombinant human interferon-α2a and interferon-α2b. The method has been set up and validated for accuracy, precision, linearity, sensitivity and specificity. A recovery test indicated a bias of less than 1% and intra-day and inter-day quantitative determinations presented relative standard deviations always < 4 %, while experimental sensitivity was 0.3 μg (RSD = 5 %). Regarding to linearity, the coefficient of determination was 0.998 (p<0.0001), for a range of analyzed interferon mass from 0,62 to 10 μg. This rapid methodology allows the application of the RP-HPLC as a powerful tool to monitor the production yield and quality of periplasmic Interferon α2 right after, or even during the fermentation. The optimum expression temperature was evaluated in flask cultures from 30 to 42 °C. It was observed that the volumetric and specific production were higher for culture temperatures equal or above 35 °C. Thus, considering the potential recombinant protein degradation induced by temperature, 35 °C was well-marked as the optimum temperature for interferon expression. The higher values for specific and volumetric production in culture flasks were 1.04 μg/mL/A600 and 3.45 mg/L respectively. As purification method, it was utilized ionic chromatography followed by size-exclusion chromatography. The final purity and mass recovery was, respectively, 95.3 % and 66 %. The final product was also characterized utilizing SDS-PAGE, western blotting, reversed-phase HPLC, size-exclusion HPLC and mass spectrometry analysis.
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Ferbus, Didier. "La (2'-5') oligoadenylate synthetase, enzyme induite par l'interferon : caracterisation et implication dans le mecanisme d'action des interferons." Paris 6, 1987. http://www.theses.fr/1987PA066370.

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Purification et caracterisation de la (2',5') oligoadenylate synthetase des reticulocytes de lapin. Role des interferons et de la (2',5') oligoadenylate synthetase dans la differenciation des lignees hematopoietiques
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GACHET, YANNICK, and Paul R. Cohen. "Purification et caracterisation d'une proteine induite apres choc thermique - comparaison avec les interferons." Paris 6, 1993. http://www.theses.fr/1993PA066096.

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Une proteine excretee de cellules epithelioides de rein de boeuf (mdbk) au cours de la periode de recuperation apres choc thermique (hsif) a ete purifie 10. 000 fois. Si ce facteur presente toujours la capacite d'induire la 25 oligoadenylate synthetase (25as), une methode plus sensible de mesure de la capacite de resister a un virus (vsv) a permis de mettre en evidence un etat antiviral induit dans des cellules traitees par le hsif. L'analyse des proteines induites dans des cellules traitees ou non par le hsif ou les interferons alpha, beta et gamma bovins a permis d'etablir que le hsif induit des proteines qui lui sont specifiques. Les gels filtrations et l'electrophorese ont montre que le hsif a un poids moleculaire de #4#5 kd ; le point isoelectrique (6,8) a ete determine par chromatofocalisation. Les etudes menees a l'aide d'anticorps polyclonaux contre les trois interferons bovins ont permis de conclure definitivement que le hsif ne presentait pas de parente antigenique avec les interferons alpha, beta et gamma bovins. De plus, l'etude menee sur les voies de transduction du hsif et des interferons alpha, beta et gamma bovins ont montre que le hsif est un interferon atypique. La 2'5' as catalyse la synthese d'un 2'5' oligoadenylate qui est le cofacteur de l'endoribonuclease l (rnase l) ; cet enzyme subit un changement de localisation concomitant a l'augmentation de l'activite de fla 2'5' as de 100 kd apres choc thermique
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Chiu, Shih-Wen, and 邱詩雯. "Expression, Purification and Activity analysis of Canine Interferon-α2." Thesis, 2012. http://ndltd.ncl.edu.tw/handle/93086561459246624637.

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碩士
國立宜蘭大學
生物技術研究所碩士班
100
The antiviral activity of type I interferon (IFN) has been well-documented. In order to clone the IFN gene, MDCK cells were treated with polyI:C for 24 hours and the cellular RNAs were extracted for RT-PCR amplification. After sequence analysis, the amplified IFN gene fragment was then cloned into prokaryotic and eukaryotic expression vectors for expressions of the recombinant canine IFN and a high molecular protein fused canine IFN respectively. To investigate the bioactivity of these recombinant proteins, MDCK cells were treated with purified recombinant protein s separately and the mRNA and protein expression levels of Mx, PKR, and OAS were examined by western blot and real-time RT-PCR at 24, 48, and 72 hours post treatment. Results showed that the IFN proteins expressed in prokaryotic expression system and high molecular protein fused IFN expressed by eukaryotic expression system induced high amounts of Mx proteins in MDCK cells, but high molecular protein fused IFN expressed in prokaryotic system did not. Prokaryotic expressed IFN, high molecular protein fused IFN, and eukaryotic expressed high molecular protein fused IFN induced low level PKR protein as the negative control group. However, Prokaryotic expressed IFN could induce significantly-high level PKR mRNA at 24 hrs post treatment. Furthermore, Prokaryotic expressed IFN and eukaryotic expressed high molecular protein fused IFN induce significantly high amounts of OAS mRNA while prokaryotic expressed high molecular protein fused IFN could not induce OAS protein and mRNA. In conclusion, both recombinant IFN and high molecular protein fused IFN proteins were able to induce the expression of different antiviral proteins in MDCK cells. Further studies are needed to validate their antiviral function in the context of viral infection
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Chen, Han-Ting, and 陳漢婷. "Production, Purification, and Antiviral activity of Porcine Interferon-α recombinant proteins." Thesis, 2008. http://ndltd.ncl.edu.tw/handle/45529516791617619958.

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碩士
國立宜蘭大學
生物技術研究所碩士班
96
Interferon (IFN) is a member of the cytokine family. Interferons are involved in antiviral, anti-cancer, and immuno-modulatory activities. Upon viral infection, host cells express interferons which also induce the expression of antiviral proteins in neighboring cells to protect the host from further viral infection. Interferons are classified into 3 types and type I interferon, IFNα/β, plays a central role in the antiviral effect of interferons. In this thesis, recombinant proteins of porcine IFN-α were produced by an E.coli prokaryotic expression system, yielding inclusion body form recombinant proteins. 2 kinds of strong denaturant, 8 M urea or 6 M guanidine hydrochloride (GdnHCl), were used to solubilize inclusion bodies. For the purification of recombinant porcine IFN-α, immobilized metal affinity chromatography (IMAC) was used. For refolding by dialysis, a gradual, linear decrease of denaturant concentration was used. Subsequently, IFN-α was assayed for enzymatic activity after solubilization of inclusion bodies, purification, and refolding. In the antiviral assay, cells were treated with either porcine IFN-α solubilized with urea or guanidine hydrochloride and inoculated in MARC-145 and ST cells with porcine reproductive and respiratory syndrome virus (PRRSV) and pseudorabies virus (PRV) respectively. Changes in viral titer with or without IFN-α pre-treatment were measured post challenge. In addition, different dosages of recombinant porcine IFN-α were assayed and the antiviral activity of IFN-α was calculated as the lowest dosage able to suppress viral proliferation. Results showed that, porcine IFN-α recombinant proteins, when solubilized by either method, could successfully inhibit PRRSV virus (RNA type) infection as well as PRV virus (DNA type) infection. Additionally, since interferon has a short half-life in serum, porcine IFN-α was fused with porcine IgG Fc in this thesis to create constructs that are more long-lived. Three different linkers composed of glycine and serine of various lengths were used to combine the IFN and the IgG Fc. Results showed that for the expression of these recombinant, fusion proteins in prokaryotic expression system, all three constructs of various linker length (GS; GSGGGGS; GGSGGSGGGGSGGGGS) could not be expressed in large quantity.
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Araújo, Lucas Quintino da Silva. "Expression, Purification and Stability Study of the Recombinant Human Interferon α-2b." Master's thesis, 2016. http://hdl.handle.net/10362/76560.

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Recombinant human interferon α-2b (rhIFNα-2b) is a widely used therapeutic protein for the treatment of viral infections such as hepatitis. Being a therapeutic protein it is only active in its native conformation so that it is important to investigate possible pathways of degradation when producing it. In this work rhIFNα-2b was subjected to four different stress conditions and the resulting products characterized with fluorescence spectroscopy, fluorescence anisotropy, circular dichroism, dynamic light scattering and scanning electron microscopy. The results showed that rhIFNα-2b loses its native conformation in all conditions in which it was tested and there was formation of aggregates. It was also made a bioactivity assay where we saw that the protein had biological activity before and after the stress conditions.
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Pereira, Mafalda Inês Apolinário. "Design of Peptides to Interfere with the RANK-TRAF6 Pathway: an Integrated Approach." Master's thesis, 2018. http://hdl.handle.net/10362/57609.

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The RANK-TRAF6 pathway is involved in osteoporosis and in the development of breast cancer. One way to inhibit this pathway is to block TRAF6’s binding to RANK using decoy peptides. It is known by experimental data that a cell-penetrating decoy peptide (cpp) based on TRAF6-binding site mTRANCE-R(1) effectively inhibits this pathway because of its high affinity to TRAF6, whereas the TRAF6-binding site mTRANCE-R(2) does not. One of the goals of this work is to validate by in silico studies the stability of TRAF6 with five peptides, containing TRAF6-binding sites in human (hPEP1, hPEP2, PepH2-hTRANCE1) and mice (mPEP1, mPEP2). The stability of TRAF6 with the different peptides was accessed with two methods. The first method uses the complexes buried surface area (BSA) values, as a higher BSA indicates a higher complex stability. The results obtained with this method are in agreement with the experimental data, suggesting that the peptide with the sequence mTRANCE-R(1) has a higher affinity to TRAF6 than the peptide with the sequence mTRANCE-R(2), indicating that it is more stable with TRAF6. BSA(mTRAF6-mPEP1) > BSA(mTRAF6-mPEP2) and BSA(hTRAF6-hPEP1) > BSA(hTRAF6-hPEP2). BSA(hTRAF6- PepH2-hTRANCE1) > BSA(hTRAF6-hPEP1). The other method uses an optimized HADDOCK score as a tool to predict binding affinity. These results are not in agreement with the literature and the ones determined by BSA studies, failing in validating the stability of TRAF6 with a peptide containing mTRANCE-R(1) and a peptide containing mTRANCE-R(2). Peptides hTRANCE-R(1) and PepH2-hTRANCE1 (>99%) were prepared by manual Fmoc solid phase peptide synthesis followed by HPLC purification. In the PepH2- hTRANCE1 synthesis, besides the desired peptide, we also isolated a side product that was identified as the same peptide sequence with a Valine deletion. This peptide will also be used for future cancer cell studies. The secondary structure of the peptides was analysed by circular dichroism, showing the same fractions of -sheet (0,4) and random coil (0,6) for all.
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Book chapters on the topic "Interferon Purification"

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Fantes, K. H. "Purification of Interferons." In Ciba Foundation Symposium - Interferon, 78–94. Chichester, UK: John Wiley & Sons, Ltd., 2008. http://dx.doi.org/10.1002/9780470719626.ch7.

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Platis, Dimitris, and Graham R. Foster. "Interferon Proteins: Structure, Production and Purification." In The Interferons, 73–83. Weinheim, FRG: Wiley-VCH Verlag GmbH & Co. KGaA, 2006. http://dx.doi.org/10.1002/3527608206.ch3.

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Novick, Daniela, Dina G. Fischer, and Menachem Rubinstein. "Purification of the Human Interferon-γ Receptor by Ligand Affinity." In Receptor Purification, 459–81. Totowa, NJ: Humana Press, 1990. http://dx.doi.org/10.1007/978-1-4612-0461-9_24.

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Tamai, T., T. Noguchi, N. Sato, S. Kimura, S. Shirahata, and H. Murakami. "Purification and cDNA Cloning of Flatfish Interferon." In Animal Cell Technology: Basic & Applied Aspects, 99–105. Dordrecht: Springer Netherlands, 1993. http://dx.doi.org/10.1007/978-94-011-2044-9_14.

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Tamai, T., T. Noguchi, K. Tsujimura, N. Sato, S. Kimura, S. Shirahata, and H. Murakami. "Mass Production and Purification of Recombinant Flatfish Interferon." In Animal Cell Technology: Basic & Applied Aspects, 123–27. Dordrecht: Springer Netherlands, 1993. http://dx.doi.org/10.1007/978-94-011-2044-9_17.

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Novick, D., P. Orchansky, M. Revel, and M. Rubinstein. "Purification and Characterization of the Receptor for Human Interferon-γ." In The Biology of the Interferon System 1986, 121–28. Dordrecht: Springer Netherlands, 1987. http://dx.doi.org/10.1007/978-94-009-3543-3_18.

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Tamai, Tadakazu, Hiroshi Oda, Nobuyuki Sato, Shigeru Moriyama, Shoji Kimura, Sanetaka Shirahata, and Hiroki Murakami. "Production, Purification and Application of Flatfish (Paralichthys olivaceus) Interferon." In Animal Cell Technology: Developments Towards the 21st Century, 449–53. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-011-0437-1_71.

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Ma, Yue, Minhui Long, and Aipo Diao. "Expression, Purification, and Activity Assay of Chicken Interferon-Alpha." In Proceedings of the 2012 International Conference on Applied Biotechnology (ICAB 2012), 741–47. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-37922-2_76.

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Pfahler, V., J. Adu-Gyamfi, D. O’Connell, and F. Tamburini. "Purification Protocol." In Oxygen Isotopes of Inorganic Phosphate in Environmental Samples, 33–44. Cham: Springer International Publishing, 2022. http://dx.doi.org/10.1007/978-3-030-97497-8_3.

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AbstractThe five stepwise purification of extracts and final precipitation of silver phosphate (A1–A5) are described. The first two steps (A1 and A2) are removing organic matter and are concentrating the phosphate in the extract by reducing the volume. Certain cations could interfere with the precipitation of silver phosphate and are removed in step A3. Silver chloride, which, if not removed, could co-precipitate with silver phosphate, is removed in step A4. The final analyte is then precipitated in step A5. The filtration steps can be quite tedious, using vacuum filtration equipment is therefore recommended. Following step A5, the silver phosphate samples need to be weighed in for the measurement with a thermal conversion elemental analyser (TC/EA) coupled to a continuous-flow isotope-ratio mass spectrometer (IRMS).
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Aydin, Omer, Dilek Kanarya, Ummugulsum Yilmaz, and Cansu Ümran Tunç. "Determination of Optimum Ratio of Cationic Polymers and Small Interfering RNA with Agarose Gel Retardation Assay." In Methods in Molecular Biology, 117–28. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2010-6_7.

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AbstractNanomaterials have aroused attention in the recent years for their high potential for gene delivery applications. Most of the nanoformulations used in gene delivery are positively charged to carry negatively charged oligonucleotides. However, excessive positively charged carriers are cytotoxic. Therefore, the complexed oligonucleotide/nanoparticles should be well-examined before the application. In that manner, agarose gel electrophoresis, which is a basic method utilized for separation, identification, and purification of nucleic acid molecules because of its poriferous nature, is one of the strategies to determine the most efficient complexation rate. When the electric field is applied, RNA fragments can migrate through anode due to the negatively charged phosphate backbone. Because RNA has a uniform mass/charge ratio, RNA molecules run in agarose gel proportional according to their size and molecular weight. In this chapter, the determination of complexation efficiency between cationic polymer carriers and small interfering RNA (siRNA) cargos by using agarose gel electrophoresis is described. siRNA/cationic polymer carrier complexes are placed in an electric field and the charged molecules move through the counter-charged electrodes due to the phenomenon of electrostatic attraction. Nucleic acid cargos are loaded to cationic carriers via the electrostatic interaction between positively charged amine groups (N) of the carrier and negatively charged phosphate groups (P) of RNA. The N/P ratio determines the loading efficiency of the cationic polymer carrier. In here, the determination of N/P ratio, where the most efficient complexation occurs, by exposure to the electric field with a gel retardation assay is explained.
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Conference papers on the topic "Interferon Purification"

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Lian, E. C. Y., and F. A. Siddigui. "BINDING OF 37-DKa PLATELET AGGLUTINATING PROTEIN TO HUMAN PLATELETS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643976.

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We have previously reported the purification of a 37-KDa platelet agglutinating protein (PAP p37) from the plasma of a patient with thrombotic thrombocytopenic purpura. using 125I-labeled p37, the properties of its binding to platelets were studied. The binding of p37 to washed human platelets from 4 normal subjects and two TTP patients after recovery was specific, concentration dependent and saturable. The Scatchard analysis revealed that the binding sites for p37 was about 100,000 per platelet with a dissociation constant of 48 × 10−9 M. The binding of p37 to erythrocytes was very little and non-specific. Stimulation of platelets by thrombin or ADP did not have any effect on the binding of p37 to platelets. The monoclonal antibodies to platelet GP lb (6D1) and GP Ilb-llla (10E5)(A gift of Dr. Barry coller) did not inhibit the binding of p37 to platelets. Fibrinogen (1 mg/ml) and FVIII/vWF (250 ug/ml) reduced the binding slightly. The polyclonal antibodies to p37 as well as concanavalin-A inhibited the binding of p37 to platelets through their direct interaction with p37. Other lectins such as phytohemagglutinin, potato lectin and helix pomatia lectin did not have any effect. At 40 mM, sialic acid, α-D-(+)-glucose, D-(+)-mannose and D-fructose caused 91%,44%,79%, and 63% inhibition of p37 binding respectively. D-(+)-galactose did not interfere with the binding. It is concluded that p37 binds to platelets on the sites other than GP lb and Gp IIb-IIIa and its binding to platelets is inhibited by certain sugars.
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Nottoli, Emmanuelle, Philippe Bienvenu, Didier Bourlès, Alexandre Labet, Maurice Arnold, and Maité Bertaux. "Determination of Long-Lived Radionuclide (10Be, 41Ca, 129I) Concentrations in Nuclear Waste by Accelerator Mass Spectrometry." In ASME 2013 15th International Conference on Environmental Remediation and Radioactive Waste Management. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/icem2013-96054.

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Radiological characterization of nuclear waste is essential for storage sites management. However, most of Long-Lived RadioNuclides (LLRN), important for long-term management, are difficult to measure since concentration levels are very low and waste matrices generally complex. In an industrial approach, LLRN concentrations are not directly measured in waste samples but assessed from scaling factors with respect to easily measured gamma emitters. Ideally, the key nuclide chosen (60Co, 137Cs) should be produced by a similar mechanism (fission or activation) as the LLRN of interest and should have similar physicochemical properties. However, the uncertainty on the scaling factors, determined from experimental and/or calculation data, can be quite important. Consequently, studies are performed to develop analytical procedures which would lead to determine precisely the concentration of LLRN in nuclear waste. In this context, the aim of this study was to determine the concentrations of three LLRN: 129I (T1/2 = 15.7×106 a), 41Ca (T1/2 = 9.94×104 a) and 10Be (T1/2 = 1.387×106 a) in spent resins used for primary fluid purification in Pressurized Water Reactors using Accelerator Mass Spectrometry (AMS) for measurement. The AMS technique combined mass spectrometry and nuclear physics to achieve highly efficient molecular and elemental isobars separation. Energies of several Million Electron-Volt transferred to the ions in the first accelerating part of specifically developed tandem accelerators lead to molecular isobars destruction through interaction with the argon gas used to strip the injected negative ions to positive ones. At the exit of the tandem accelerator, the energy acquired in both accelerating parts allows an elemental isobars separation based on their significantly different energy loss (dE) while passing through a thickness of matter dx that is proportional to their atomic number (Z) and inversely proportional to ions velocity (ν) according to the Bethe-Block law (1). (1)dEdx=k*Z2ν2 The use of a particle accelerator in conjunction with a selective ion source, mass and energy filters and a high-performance detector thus allow unambiguously identifying and measuring analyte concentration against much more abundant interfering isobars. The development of AMS and of related applications have recently been extensively reviewed [1–3]. Up to now, the potentialities of the accelerator mass spectrometry technique were explored for the measurement of cosmogenic radionuclides produced in the Earth’s environment either in the atmosphere or in the Earth’s crust (in situ-production). Many applications aiming to date and/or quantify Earth surface processes have been developed in the fields of geology, geomorphology and planetary sciences as well as archeology paleoanthropology and biomedicine. The present study extends the scope of AMS to nuclear industry. Because AMS facilities are not widely accessible and difficult to handle, LLRN concentrations in nuclear waste are usually determined using Inductively Coupled Plasma Mass Spectrometry (ICP-MS) and radiometric techniques. However for the measurement of very low LLRN concentrations, AMS becomes the most effective measurement method with detection limits of 105–106 atoms per sample. In this study, AMS measurements were performed using the French AMS national facility ASTER located at the Centre Européen de Recherche et d’Enseignement des Géosciences de l’Environnement (CEREGE). The challenge was to define a chemical treatment procedure allowing the measurement of the three nuclides, 10Be, 41Ca and 129I, by AMS. Each method selection was based on three main requirements: 1) a quantitative recovery in solution of Be, Ca, I and key radionuclides after resin mineralization, 2) a selective extraction from the sample matrix and the separation from β-γ emitters (3H, 14C, 55Fe, 59Ni, 60Co, 63Ni, 90Sr, 125Sb, 134Cs, 137Cs) and isobars, 3) the precipitation of each element under the best suited forms (i.e. AgI, CaF2, BeO) for AMS measurements. The chosen methods were optimized on synthetic solutions and finally applied for the determination of the three LLRN concentrations in spent resins from a 900 MWe Nuclear Power Reactor.
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Reports on the topic "Interferon Purification"

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Joyce, Christine, and Deidre Mountain. Optimization of Liposomal Encapsulation Efficiency. University of Tennessee Health Science Center, 2021. http://dx.doi.org/10.21007/com.lsp.2018.0002.

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Introduction: My project was a continuation of the Vascular Research Lab’s (VRL) ongoing research at the University of Tennessee Medical Center Knoxville (UTMCK) aimed at optimizing liposomal encapsulation efficiency of small interfering RNA (siRNA) which can be used to silence genes to prevent a variety of disease pathologies. Methods: Assay siRNA loading capacity of liposomes based on lipid concentration Development of a method for liposome purification: HPLC & HiTRAP Column Results & Conclusion: siRNA loading capacity Higher lipid:siRNA resulted in increased encapsulation efficiency HPLC – did not work as expected HiTRAP Column – currently being optimized to be used as part of standard operating procedures
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