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1.

001-es BibID:BIBFORM122537
035-os BibID:(Scopus)85197084238 (WoS)001259901900001
Első szerző:Auer, Felicia
Cím:In Migratio Noncovalent Fluorophore Labeling of Proteins by Propidium Iodide in Sodium Dodecyl Sulfate Capillary Gel Electrophoresis / Auer Felicia, Guttman Andras
Dátum:2024
ISSN:0003-2700
Megjegyzések:Sodium dodecyl sulfate capillary gel electrophoresis is one of the frequently used methods for size-based protein separation in molecular biology laboratories and the biopharmaceutical industry. To increase throughput, quite a few multicapillary electrophoresis systems have been recently developed, but most of them only support fluorescence detection, requiring fluorophore labeling of the sample proteins. To avoid the time-consuming derivatization reaction, we developed an on-column labeling approach utilizing propidium iodide for the first time in SDS-CGE of proteins, a dye only used before for nucleic acid analysis. As a key ingredient of the gel-buffer system, the oppositely migrating positively charged propidium ligand in migratio complexes with the SDS-proteins, therefore, supports in situ labeling during the electrophoretic separation process, not requiring any extra pre- or postcolumn derivatization step. A theoretical treatment is given to shed light on the basic principles of this novel online labeling process, also addressing the influence of propidium iodide on the electroosmotic flow, resulting in reduced retardation. The concept of propidium labeling in SDS-CGE was first demonstrated using a commercially available protein sizing ladder ranging from 6.5 to 200 kDa with different isoelectric points and post-translational modifications. Considering the increasing number of protein therapeutics on the market next, we focused on the labeling optimization of a therapeutic monoclonal antibody and its subunits, including the addition of the nonglycosylated heavy chain. Peak efficiency and resolution were compared between noncovalent and covalent labeling. The effect of ligand concentration on the effective and apparent electrophoretic mobility, the resulting peak area, and the resolution were all evaluated in view of the theoretical considerations. The best detection sensitivity for the intact monoclonal antibody was obtained by using 200 ?g/mL propidium iodide in the separation medium (LOD 2 ?g/mL, 1.35 ? 10-8 M) with excellent detection linearity over 3 orders of magnitude. On the other hand, the resolution between the biopharmaceutical protein test mixture components containing the intact and subunit fragments of the therapeutic monoclonal antibody was very good in the ligand concentration range of 50-200 ?g/mL, but using the local maximum at 100 ?g/mL for the nonglycosylated/glycosylated heavy chain pair is recommended. The figures of merit, including precision, sensitivity, detection linear range, and resolution for a sample mixture in hand, can be optimized by varying the propidium iodide concentration in the gel-buffer system, as demonstrated in this paper.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Analytical Chemistry. - 96 : 27 (2024), p. 10969-10977. -
További szerzők:Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:TUDFIN
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2.

001-es BibID:BIBFORM043661
035-os BibID:(WoS)000285215800035 (Scopus)78650351800
Első szerző:Bones, Jonathan
Cím:Ultra Performance Liquid Chromatographic Profiling of Serum N-Glycans for Fast and Efficient Identification of Cancer Associated Alterations in Glycosylation / Bones Jonathan, Mittermayr Stefan, O'Donoghue Niaobh, Guttman András, Rudd Pauline M.
Dátum:2010
ISSN:0003-2700
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
biopharmaceutical
Megjelenés:Analytical Chemistry. - 82 : 24 (2010), p. 10208-10215. -
További szerzők:Mittermayr, Stefan (1983-) (bioinformatikus) O'Donoghue, Niaobh Guttman András (1954-) (vegyészmérnök) Rudd, Pauline M.
Pályázati támogatás:EU FP6 GLYFDIS 037661
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3.

001-es BibID:BIBFORM092907
035-os BibID:(WoS)000584418100065 (Scopus)85096830637
Első szerző:Drouin, Nicolas
Cím:Capillary Electrophoresis-Mass Spectrometry at Trial by Metabo-Ring: Effective Electrophoretic Mobility for Reproducible and Robust Compound Annotation / Nicolas Drouin, Marlien van Mever, Wei Zhang, Elena Tobolkina, Sabrina Ferre, Anne-Catherine Servais, Marie-Jia Gou, Laurent Nyssen, Marianne Fillet, Guinevere S. M. Lageveen-Kammeijer, Jan Nouta, Andrew J. Chetwynd, Iseult Lynch, James A. Thorn, Jens Meixner, Christopher Lößner, Myriam Taverna, Sylvie Liu, N. Thuy Tran, Yannis Francois, Antony Lechner, Reine Nehmé, Ghassan AlHamoui Dit Banni, Rouba Nasreddine, Cyril Colas, Herbert H. Lindner, Klaus Faserl, Christian Neusüß, Manuel Nelke, Stefan Lämmerer, Catherine Perrin, Claudia Bich-Muracciole, Coral Barbas, Ángeles López Gonzálvez, Andras Guttman, Marton Szigeti, Philip Britz-McKibbin, Zachary Kroezen, Meera Shanmuganathan, Peter Nemes, Erika P. Portero, Thomas Hankemeier, Santiago Codesido, Víctor González-Ruiz, Serge Rudaz, Rawi Ramautar
Dátum:2020
ISSN:0003-2700
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Analytical Chemistry. - 92 : 20 (2020), p. 14103-14112. -
További szerzők:van Mever, Marlien Zhang, Wei Tobolkina, Elena Ferre, Sabrina Servais, Anne-Catherine Gou, Marie-Jia Nyssen, Laurent Fillet, Marianne Lageveen-Kammeijer, Guinevere S. M. Nouta, Jan Chetwynd, Andrew J. Lynch, Iseult Thorn, James A. Meixner, Jens Lößner, Christopher Taverna, Myriam Liu, Sylvie Tran, N. Thuy Francois, Yannis Lechner, Antony Nehmé, Reine AlHamoui Dit Banni, Ghassan Nasreddine, Rouba Colas, Cyril Lindner, Herbert H. Faserl, Klaus Neusüß, Christian Nelke, Manuel Lämmerer, Stefan Perrin, Catherine Bich-Muracciole, Claudia Barbas, Coral Gonzálvez, Ángeles López Guttman András (1954-) (vegyészmérnök) Szigeti Márton (1986-) (környezetmérnök) Britz-McKibbin, Philip Kroezen, Zachary Shanmuganathan, Meera Nemes Péter Portero, Erika P. Hankemeier, Thomas Codesido, Santiago González-Ruiz, Víctor Rudaz, Serge Ramautar, Rawi
Pályázati támogatás:NKFIH NN127062
egyéb
2018-2.1.17-TÉT-KR-2018-00010
egyéb
BIONANO_GINOP-2.3.2-15-2016-00017
GINOP
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4.

001-es BibID:BIBFORM121603
035-os BibID:(Scopus)85194393047 (WoS)001248542600001
Első szerző:Farsang Róbert
Cím:Glucose unit computation in capillary zone electrophoresis of carbohydrates using a numerical approximation based search for a virtual EOF marker. A tutorial / Robert Farsang, Anna Farkas, Gábor Jarvas, András Guttman
Dátum:2024
ISSN:0165-9936
Megjegyzések:Several high-resolution carbohydrate separation methods are currently available for structural elucidation in the analytical glycomics field, but the associated glyco-informatics support is lagging. Identifying protein-bound glycan structures represents a multifaceted challenge with elements of separation science, bioinformatics, and sophisticated computational methods. In electroosmotic flow (EOF) driven separations with counter currently migrating sample components, the apparent migration times of the analyte molecules are the result of the interplay between their effective electrophoretic mobilities and the EOF. The resulting continuously increasing migration time distances between the consecutively migrating maltodextrin oligomers make glucose unit value calculation and the subsequent structural interpretation of unknown glycans extremely challenging. To correct this irregularity, a numerical approximation-based search-derived virtual electroosmotic flow marker is introduced and utilized. This tutorial guides the reader through the computation process for structural elucidation of N-linked carbohydrates by using a detailed worked example with a monoclonal antibody of biopharmaceutical interest.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Carbohydrates
Capillary electrophoresis
Virtual EOF marker
Numerical approximation
Maltodextrin ladder
Glucose unit
Megjelenés:Trac-Trends In Analytical Chemistry. - 176 (2024), p. 1-9. -
További szerzők:Farkas Anna (1988-) (molekuláris biológus) Járvás Gábor (1982-) (vegyészmérnök) Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:2023-1.2.1-ERA_NET-2023-00015
Egyéb
1G3DBK0CTUF247
Egyéb
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Intézményi repozitóriumban (DEA) tárolt változat
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5.

001-es BibID:BIBFORM116213
035-os BibID:(WoS)001104988800001 (Scopus)85178183698
Első szerző:Farsang Róbert
Cím:Capillary Zone Electrophoresis of 8-Aminopyrene-1,3,6-trisulfonic Acid Labeled Carbohydrates with Online Electrokinetic Sample Cleanup / Farsang Robert, Hogyor Kinga, Jarvas Gabor, Guttman Andras
Dátum:2023
ISSN:0003-2700
Megjegyzések:Capillary electrophoresis is one of the frequently used separation techniques for the analysis of complex carbohydrates. Since sugars lack chromophore or fluorophore groups, their capillary electrophoresis analysis usually requires tagging by a charged fluorophore. To speed up the derivatization reaction, a large excess of the labeling reagent is typically used; therefore, a purification step is necessary prior to CE analysis using the industry standard low-pH gel-buffer system. In addition to representing an extra sample preparation step with the associated labor and cost, the purification process also holds the risk of losing some of the sample components. In this paper we introduce an online electrokinetic sample cleanup process with electroosmotic flow (EOF)-assisted separation in a bare fused silica capillary using alkaline pH background electrolyte and normal polarity separation voltage. 8-Aminopyrene-1,3,6-trisulfonic acid (APTS)-labeled maltooligosaccharides were analyzed first to understand the complex effect of the downstream EOF and the counter current electromigration of the sample components including the labeling dye. The use of 150 mM caproic acid?253 mM Tris (pH 8.1) running buffer facilitated the entrance of the sample components of interest into the separation capillary, while the excess labeling reagent was excluded and, therefore, did not interfere with the detection. The alkaline caproic acid?Tris running buffer was then applied to the N-glycome analysis of human serum samples, showing excellent separation performance, and more importantly, the extra sample purification step was not required.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Capillary electrophoresis
Carbohydrates
Electroosmosis
Labeling
Polarity
Megjelenés:Analytical Chemistry. - 95 : 45 (2023), p. 16459-16464. -
További szerzők:Hogyor Kinga Járvás Gábor (1982-) (vegyészmérnök) Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:DE TUDFIN
Egyéb
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6.

001-es BibID:BIBFORM106835
035-os BibID:(Scopus)85138605879 (WoS)000856676100001
Első szerző:Filep Csenge Boróka (biomérnök)
Cím:Electromigration Dispersion in Sodium Dodecyl Sulfate Capillary Gel Electrophoresis of Proteins / Filep Csenge, Guttman András
Dátum:2022
ISSN:0003-2700
Megjegyzések:The electromigration dispersion of the light- and heavy-chain subunit peaks of the therapeutic monoclonal antibody omalizumab was investigated in sodium dodecyl sulfate capillary gel electrophoresis (SDS?CGE) using borate cross-linked dextran sieving matrices. Increasing boric acid content (340?640 mM) caused electromigration dispersion shifts for both low (2%)- and high (10%)-dextran-concentration gels in all gel?buffer compositions. In case of the heavy-chain fragment, elevated borate concentrations resulted in decreasing tailing and increasing fronting with the use of higher- and lower-dextranconcentration gels, respectively. The light-chain fragment, on the other hand, exhibited increased fronting with increasing borate concentration for both dextran concentrations examined in this study. Increase of the glycerol ingredient level in the gel?buffer system caused the same effect as the increasing borate concentration in both dextran concentrations. The detected electromigration dispersion was considered as the result of the formation of monomeric and dimeric glycerol-borate complexes as co-ionic constituents, migrating slower than that of the unconjugated tetrahydroxyborate. In addition, complexation of the tetrahydroxyborate anion with the glucose building blocks of the dextran polymer decreased its mobility to practically zero, contributing to further decrease in the resultant effective mobility of the co-ionic species. We suggest that the observed fronting and/or tailing peak shapes of the monoclonal antibody fragments in SDS?CGE at increasing boric acid concentrations can be considered as the result of multiple effects including changes in pH, sieving matrix pore size, viscosity, and the mobility variation of the co-ionic borate adducts with the gel?buffer ingredients. While electromigration dispersion-mediated band broadening, in general, can be minimized via matching the effective mobility of the co-ionic species to the analyte molecules of interest, in case of borate cross-linked dextran gels, optimization of the boric acid concentration required special consideration of its gel cross-linking function. For the light- and heavy-chain fragments of the IgG analyte, best peak shapes were attained with the use of 10% dextran/340 mM boric acid and 10% dextran/640 mM boric acid-containing gel?buffer systems, respectively. Based on this observation, here we introduce the concept of borate-gradient-mediated transient mobility matching in SDS?CGE of proteins. This novel approach resulted in close to optimal peak shapes for the distantly migrating IgG subunits within a single run, as well as unraveled the long-sought possible solution to perform capillary pore-size-gradient gel electrophoresis.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Analytical Chemistry. - 94 : 38 (2022), p. 13092-13099. -
További szerzők:Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:EFOP-3.6.3-VEKOP-16-2017-00009
EFOP
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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7.

001-es BibID:BIBFORM093742
035-os BibID:(WoS)000623041000027 (Scopus)85100632127
Első szerző:Filep Csenge Boróka (biomérnök)
Cím:Effect of the Monomer Cross-Linker Ratio on the Separation Selectivity of Monoclonal Antibody Subunits in Sodium Dodecyl Sulfate Capillary Gel Electrophoresis / Csenge Filep, András Guttman
Dátum:2021
ISSN:0003-2700
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Analytical Chemistry. - 93 : 7 (2021), p. 3535-3541. -
További szerzők:Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:2.3.2-15-2016-00017
GINOP
NKFIH
Egyéb
ÚNKP-20-3-II-DE-294
Egyéb
2020-4.1.1-TKP2020
Egyéb
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8.

001-es BibID:BIBFORM083893
035-os BibID:(WoS)000518234700070 (Scopus)85080047360
Első szerző:Filep Csenge Boróka (biomérnök)
Cím:The Effect of Temperature in Sodium Dodecyl Sulfate Capillary Gel Electrophoresis of Protein Therapeutics / Filep Csenge, Guttman András
Dátum:2020
ISSN:0003-2700
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Analytical Chemistry. - 92 : 5 (2020), p. 4023-4028. -
További szerzők:Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:2.3.2-15-2016-00017
GINOP
NKFIH NN 127062
Egyéb
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9.

001-es BibID:BIBFORM096076
035-os BibID:(WoS)000672115800032 (Scopus)85110405663
Első szerző:Guttman András (vegyészmérnök)
Cím:Fundamentals of Capillary Electrophoretic Migration and Separation of SDS Proteins in Borate Cross-Linked Dextran Gels / András Guttman, Csenge Filep, Barry L. Karger
Dátum:2021
ISSN:0003-2700
Megjegyzések:Abstract Abstract Image Recent progress in the development and production of new, innovative protein therapeutics require rapid and adjustable high-resolution bioseparation techniques. Sodium dodecyl sulfate capillary gel electrophoresis (SDS-CGE) using a borate (B) cross-linked dextran (D) separation matrix is widely employed today for rapid consistency analysis of therapeutic proteins in manufacturing and release testing. Transient borate cross-linking of the semirigid dextran polymer chains leads to a high-resolution separation gel for SDS?protein complexes. To understand the migration and separation basis of the D/B gel, the present work explores various gel formulations of dextran monomer (2, 5, 7.5, and 10%) and borate cross-linker (2 and 4%) concentrations. Ferguson plots were analyzed for a mixture of protein standards with molecular weights ranging from 20 to 225 kDa, and the resulting nonlinear concave curves pointed to nonclassical sieving behavior. While the 2% D/4% B gel resulted in the fastest analysis time, the 10% D/2% B gel was found to produce the greatest separation window, even higher than with the 10% D/4% B gel, due to a significant increase in the electroosmotic flow of the former composition in the direction opposite to SDS?protein complex migration. The study then focused on SDS-CGE separation of a therapeutic monoclonal antibody and its subunits. A combination of molecular weight and shape selectivity as well as, to a lesser extent, surface charge density differences (due to glycosylation on the heavy chain) influenced migration. Greater molecular weight selectivity occurred for the higher monomer concentration gels, while improved glycoselectivity was obtained using a more dilute gel, even as low as 2% D/2% B. This latter gel took advantage of the dextran?borate?glycoprotein complexation. The study revealed that by modulating the dextran (monomer) and borate (cross-linker) concentration ratios of the sieving matrix, one can optimize the separation for specific biopharmaceutical modalities with excellent column-to-column, run-to-run, and gel-to-gel migration time reproducibilities (<0.96% relative standard deviation (RSD)). The widely used 10% dextran/4% borate gel represents a good screening option, which can then be followed by a modified composition, optimized for a specific separation as necessary.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Analytical Chemistry. - 93 : 26 (2021), p. 9267-9276. -
További szerzők:Filep Csenge Boróka (1993-) (biomérnök) Karger, Barry
Pályázati támogatás:2.3.2- 15-2016-00017
GINOP
NKFIH (NN 127062)
Egyéb
ÚNKP-20-3-II-DE-294
Egyéb
2020-4.1.1-TKP2020
Egyéb
Internet cím:DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

10.

001-es BibID:BIBFORM065042
035-os BibID:(WoS)000365931100006 (Scopus)84948451094
Első szerző:Guttman András (vegyészmérnök)
Cím:Effect of Separation Temperature on Structure Specific Glycan Migration in Capillary Electrophoresis / Andras Guttman, Marta Kerekgyarto, Gabor Jarvas
Dátum:2015
ISSN:0003-2700
Megjegyzések:Temperature dependent differential migration shifts were studied in capillary electrophoresis between linear (maltooligosaccharides) and branched (sialylated, neutral and core fucosylated biantennary IgG glycans) carbohydrates. Background electrolytes without as well as with low and high molecular weight additives (ethylene glycol, linear polyacrylamide and poly(ethylene oxide)) were investigated for this phenomena in the temperature range of 20-50 ?C. Glucose unit (GU) value shifts were observed with increasing temperature for the all IgG glycans both in additive-free and additive-containing background electrolytes, emphasizing the importance of tight temperature control during glycosylation analysis by capillary electrophoresis. The activation energy concept was applied to understand the structure specific electrophoretic migration of the different sugar molecules. Activation energy values were derived from the slopes of the Arrhenius plots of logarithmic mobility vs reciprocal absolute temperature and compared for the linear and branched sugars as well as for the various background electrolyte additives.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
capillary electrophoresis
glycan structure
mobility
temperature
activation energy
Megjelenés:Analytical Chemistry. - 87 : 23 (2015), p. 11630-11634. -
További szerzők:Kerékgyártó Márta (1987-) (molekuláris biológus) Járvás Gábor (1982-) (vegyészmérnök)
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11.

001-es BibID:BIBFORM111410
035-os BibID:(scopus)85150484493 (wos)000961434700001
Első szerző:Hajba László
Cím:Capillary Gel Electrophoresis of Proteins : Historical overview and recent advances / Hajba László, Jeong Sunkyung, Chung Doo Soo, Guttman András
Dátum:2023
ISSN:0165-9936
Megjegyzések:This review summarizes the fundamental principles, basic methodologies, strength and weaknesses of capillary gel electrophoresis of proteins by providing both a short historical overview and highlighting new developments and applications in biopharmaceutical, biomedical as well as food and agriculture fields. The subsets of the method including native capillary gel electrophoresis, SDS capillary gel electrophoresis, capillary gel isoelectric focusing, capillary gel isotachophoresis and capillary affinity gel electrophoresis of proteins are all critically reviewed. Relevant protein labeling techniques are also addressed.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Trac-Trends In Analytical Chemistry. - 162 (2023), p. 1-12. -
További szerzők:Jeong, Sunkyung Chung, Doo Soo Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:2018?2.1.17-TÉT-KR-2018-00010
Egyéb
2019?2.1.11-TÉT-2019-00068
Egyéb
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12.

001-es BibID:BIBFORM099678
035-os BibID:(WoS)000512868300001 (Scopus)85079034813
Első szerző:Hajba László
Cím:Recent Advances in Capillary Electrochromatography of Proteins and Carbohydrates in the Biopharmaceutical and Biomedical Field / Hajba, L., Guttman, A.
Dátum:2021
ISSN:1040-8347
Megjegyzések:Capillary electrochromatography (CEC) is a powerful hybrid separation technique that combines capillary electrophoresis and capillary chromatography, capable to address the analytical challenges of proteomics and glycomics. The focus of this paper is to review the recent developments in capillary electrochromatography of proteins and carbohydrates. The different column types applied in capillary electrochromatography such as packed bed, open tubular and monoliths are conferred in detail with respective separation examples. A comprehensive comparison is also given listing the mostly utilized coating methods, stationary phase materials and column preparation methods. The choice of porogenic solvent combinations for monolithic column fabrication is thoroughly discussed, paying close attention to the fine tuning options for the separation driving electroosmotic flow. Application examples of CEC in process analytical technology for the biopharmaceutical and biomarker discovery in the biomedical fields are also given.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Critical Reviews In Analytical Chemistry. - 51 : 3 (2021), p. 289-298. -
További szerzők:Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:EFOP-3.6.3-VEKOP-16-2017-00009
EFOP
BIONANO_GINOP-2.3.2-15-2016-00017
Egyéb
NN 127062
NKFIH
K 116263
NKFIH
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Intézményi repozitóriumban (DEA) tárolt változat
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