TY - JOUR AU - Kovács, Zita AU - Bálint, Emese-Éva AU - Lászlo, Szilvia AU - Albert, Beáta AU - Gyöngyi, Tar AU - Attila, András AU - Salamon, Pál Attila TI - THE EFFECT OF SARS-COV-2 VIRUS ON THE ACTIVITY OF THE PANOPTOSIS PATHWAY IN UPPER RESPIRATORY EPITHELIAL CELLS: CORRELATIONS BETWEEN EXPRESSION PATTERNS, AGE, GENDER, AND COMORBIDITIES JF - ACTA MARISIENSIS: SERIA MEDICA J2 - ACTA MARISIEN VL - 69 PY - 2023 IS - Suppl. 5 SP - 35 EP - 35 PG - 1 SN - 2668-7755 UR - https://m2.mtmt.hu/api/publication/34109004 ID - 34109004 LA - English DB - MTMT ER - TY - JOUR AU - Salamon, Pál Attila AU - Orbán, Kálmán Csongor AU - Molnar-Nagy, Katalin AU - Kovács, Zita AU - Vancsa, Klara AU - Bálint, Emese-Éva AU - Miklossy, Ildiko AU - Albert, Beáta AU - Tar, Gyongyi AU - Lanyi, Szabolcs TI - Study of native SMAC protein production in the pUbiq expression system: Molecular cloning, biosynthesis and molecular modelling JF - ELECTRONIC JOURNAL OF BIOTECHNOLOGY J2 - ELECTRON J BIOTECHN VL - 56 PY - 2022 SP - 39 EP - 46 PG - 8 SN - 0717-3458 DO - 10.1016/j.ejbt.2022.01.0020717-3458 UR - https://m2.mtmt.hu/api/publication/33345866 ID - 33345866 AB - Background: In the process of recombinant protein biosynthesis affinity tags are efficient tools to achieve the expected purity and yield during the purification steps. Nonetheless these tags might alter enzyme specificity and activity, therefore in functional assays it is recommended to use authentic or native proteins. Several ubiquitin fusion systems have been developed for E. coli-based recombinant protein expression that provide high levels of expression, with simple purification, and allow the production of various proteins with authentic N-terminus for subsequent applications. Results: In the present research, we describe an ubiquitin fused bacterial biosynthetic system (pUbiq) for the production of the native Second mitochondria-derived activator of caspases (SMAC) recombinant protein. Using this system, the recombinant protein is expressed with an ubiquitin-decahistidine fusion partner, then purified from the cell-forming proteins by affinity chromatography. The fusion partner is then removed by proteolytic digestion, resulting the native structure of the recombinant protein without unnecessary amino acid residues. Following proteolysis, another affinity chromatography method is used to separate the native protein from the fusion partner and the proteolytic enzyme. The folding of the protein of interest was verified by a pull-down assay. Conclusions: Based on our results, the presented pUbiq system was successfully applied in the production of native SMAC recombinant protein, where the affinity tag required for purification was completely removed. Our study suggests that the ubiquitin-fusion technology will be useful for enhancing expression and purification of native and authentic proteins for structural and functional studies as well as for therapeutic uses. How to cite: Salamona P, Orbana CK, Molnar-Nagy K, et al. Exon based amplified polymorphism (EBAP): A novel and universal molecular marker for plants. Electron J Biotechnol 2022;56. https://doi.org/10.10 16/j.ejbt.2022.01.002. (c) 2022 Universidad Catolica de Valparaiso. Production and hosting by Elsevier B.V. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). LA - English DB - MTMT ER - TY - JOUR AU - Nagy, Katalin AU - Kovács, Zita AU - Miklóssy, Ildikó AU - Salamon, Pál Attila AU - Orbán, Kálmán Csongor AU - Albert, Beáta AU - Lányi, Szabolcs TI - Detergent aided refolding and purification of recombinant XIAP from inclusion bodies JF - STUDIA UNIVERSITATIS BABES-BOLYAI CHEMIA J2 - STUD UNIV BABES-BOLYAI CHEM VL - 66 PY - 2021 IS - 4 SP - 355 EP - 368 PG - 14 SN - 1224-7154 DO - 10.24193/subbchem.2021.4.26 UR - https://m2.mtmt.hu/api/publication/32547005 ID - 32547005 LA - English DB - MTMT ER - TY - JOUR AU - Nagy, Katalin AU - Kovács, Zita AU - Salamon, Pál Attila AU - Orbán, Kálmán Csongor AU - Lányi, Szabolcs AU - Albert, Beáta TI - ENHANCED HETEROLOGOUS EXPRESSION IN E. COLI JF - STUDIA UNIVERSITATIS BABES-BOLYAI CHEMIA J2 - STUD UNIV BABES-BOLYAI CHEM VL - 64 PY - 2019 IS - 2 SP - 101 EP - 110 PG - 10 SN - 1224-7154 DO - 10.24193/subbchem.2019.2.09 UR - https://m2.mtmt.hu/api/publication/30765654 ID - 30765654 N1 - University POLITEHNICA of Bucharest, Faculty of Applied Chemistry and Materials Science, Str. Gh. Polizu, Nr. 1-7, Sector 1, Bucuresti, 011061, Romania University of Pécs, Faculty of Sciences, Ifjúság útja 6, Pécs, 7624, Hungary SAPIENTIA Hungarian University of Transylvania, Faculty of Economics, Socio-Human Sciences and Engineering, Department of Bioengineering, 1 Libertatii Square, Miercurea Ciuc, RO-530104, Romania Export Date: 4 November 2019 Correspondence Address: Orbán, C.-K.; SAPIENTIA Hungarian University of Transylvania, Faculty of Economics, Socio-Human Sciences and Engineering, Department of Bioengineering, 1 Libertatii Square, Romania; email: orbancsongor@uni.sapientia.ro AB - Apoptotic regulation has been implicated in many human diseases, including cancer, autoimmune disease, inflammation and neuro degradation. Mapping up critical apoptosis regulators is a strategy for the development of new therapies [1, 2].Present work highlights optimization of heterologous expression conditions for the X-linked inhibitor of apoptosis protein (XIAP). Genes of target protein containing pGEX-4T vector was transformed in chemically competent E. coli Rosetta (TM)(DE3)pLysS cells. The recombinant construct contained a glutathione S-transferase (GST) fusion partner, which assured the purification of the protein by affinity chromatography. In the next step we examined the growth dynamics of the expression culture in M9 minimal medium, meanwhile we also determined the appropriate time of induction. Following this we carried out the optimization of expression, examining the expression's effectiveness under different conditions. On the basis of these fermentation experiments the target protein expression was the most prominent at 18 degrees C with 0.2 mM IPTG induction for 12 hours. During large scale fermentation experiments, we followed the optical density (OD), dry cell weight and substrate utilization. Finally, recombinant protein expression inhancement in the presence of 3% ethanol was successfully achieved in bioreactor. In this case the target protein was expressed in inclusion bodies, therefore solubilisation and refolding is necessary. LA - English DB - MTMT ER - TY - CONF AU - Salamon, Pál Attila AU - Nagy, Katalin AU - Kovács, Zita AU - Albert, Beáta AU - Miklóssy, Ildikó AU - Lányi, Szabolcs AU - Orbán, Csongor Kálmán ED - Majdik, Cornelia TI - Nekroptózist moduláló humán fehérjék bioszintézise T2 - XXIV. Nemzetközi Vegyészkonferencia PB - Erdélyi Magyar Műszaki Tudományos Társaság (EMT) T3 - Nemzetközi Vegyészkonferencia, ISSN 1843-6293 PY - 2018 SP - 42 UR - https://m2.mtmt.hu/api/publication/31356181 ID - 31356181 LA - Hungarian DB - MTMT ER - TY - JOUR AU - Kovács, Zita AU - Simonné Sarkadi, Livia AU - Vashegyi, Ildikó AU - Kocsy, Gábor TI - Different Accumulation of Free Amino Acids during Short- and Long-Term Osmotic Stress in Wheat JF - SCIENTIFIC WORLD JOURNAL J2 - SCI WORLD J VL - 2012 PY - 2012 PG - 10 SN - 1537-744X DO - 10.1100/2012/216521 UR - https://m2.mtmt.hu/api/publication/2053930 ID - 2053930 N1 - WoS:hiba:000308327200001 2020-08-26 23:47 cikkazonosító nem egyezik Department of Applied Biotechnology and Food Science, Budapest University of Technology and Economics, P.O. Box 91, 1521 Budapest, Hungary Agricultural Institute, Centre for Agricultural Research, Hungarian Academy of Sciences, P.O. Box 19, 2462 Martonvsr, Hungary Research Institute of Chemical and Process Engineering, Faculty of Information Technology, University of Pannonia, P.O. Box 158, 8200 Veszprém, Hungary Cited By :24 Export Date: 18 January 2021 Correspondence Address: Simon-Sarkadi, L.; Department of Applied Biotechnology and Food Science, Budapest University of Technology and Economics, P.O. Box 91, 1521 Budapest, Hungary; email: sarkadi@mail.bme.hu Chemicals/CAS: amino acid, 65072-01-7; asparagine, 70-47-3, 7006-34-0; aspartic acid, 56-84-8, 6899-03-2; glutamic acid, 11070-68-1, 138-15-8, 56-86-0, 6899-05-4; glutamine, 56-85-9, 6899-04-3; leucine, 61-90-5, 7005-03-0; macrogol, 25322-68-3; serine, 56-45-1, 6898-95-9; threonine, 36676-50-3, 72-19-5 Funding details: Seventh Framework Programme, FP7, 203288 Department of Applied Biotechnology and Food Science, Budapest University of Technology and Economics, P.O. Box 91, 1521 Budapest, Hungary Agricultural Institute, Centre for Agricultural Research, Hungarian Academy of Sciences, P.O. Box 19, 2462 Martonvsr, Hungary Research Institute of Chemical and Process Engineering, Faculty of Information Technology, University of Pannonia, P.O. Box 158, 8200 Veszprém, Hungary Cited By :27 Export Date: 28 June 2021 Correspondence Address: Simon-Sarkadi, L.; Department of Applied Biotechnology and Food Science, P.O. Box 91, 1521 Budapest, Hungary; email: sarkadi@mail.bme.hu Department of Applied Biotechnology and Food Science, Budapest University of Technology and Economics, P.O. Box 91, 1521 Budapest, Hungary Agricultural Institute, Centre for Agricultural Research, Hungarian Academy of Sciences, P.O. Box 19, 2462 Martonvsr, Hungary Research Institute of Chemical and Process Engineering, Faculty of Information Technology, University of Pannonia, P.O. Box 158, 8200 Veszprém, Hungary Cited By :27 Export Date: 29 June 2021 Correspondence Address: Simon-Sarkadi, L.; Department of Applied Biotechnology and Food Science, P.O. Box 91, 1521 Budapest, Hungary; email: sarkadi@mail.bme.hu Department of Applied Biotechnology and Food Science, Budapest University of Technology and Economics, P.O. Box 91, 1521 Budapest, Hungary Agricultural Institute, Centre for Agricultural Research, Hungarian Academy of Sciences, P.O. Box 19, 2462 Martonvsr, Hungary Research Institute of Chemical and Process Engineering, Faculty of Information Technology, University of Pannonia, P.O. Box 158, 8200 Veszprém, Hungary Cited By :27 Export Date: 1 July 2021 Correspondence Address: Simon-Sarkadi, L.; Department of Applied Biotechnology and Food Science, P.O. Box 91, 1521 Budapest, Hungary; email: sarkadi@mail.bme.hu LA - English DB - MTMT ER -