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1.

001-es BibID:BIBFORM111410
035-os BibID:(cikkazonosító)117024 (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
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2.

001-es BibID:BIBFORM085926
035-os BibID:(WoS)000401383500004 (Scopus)85015805306
Első szerző:Hajba László
Cím:Recent advances in column coatings for capillary electrophoresis of proteins / Hajba Laszlo, Guttman Andras
Dátum:2017
ISSN:0165-9936
Megjegyzések:Capillary coatings effectively improve the separation performance of proteins in capillary electrophoresis, mainly by reducing protein adsorption onto the inner capillary wall and by regulating the electroosmotic flow (EOF) to accommodate the separation problem in hand. In the first part of this review the newest trends in dynamic and permanent capillary coatings are summarized and discussed in detail. In the second part the application of nanomaterials as novel capillary coating materials is conversed. Nanomaterials have great potential in capillary coating preparations based on their advantageous properties such as large surface-to-volume ratios and a wide variety of chemistry options. Finally, some future prospective of capillary coatings in the emerging field of proteomics are given.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
capillary coating
dynamic coating
permanent coating
nanomaterials
protein separation
Megjelenés:Trac-Trends In Analytical Chemistry. - 90 (2017), p. 38-44. -
További szerzők:Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:2.3.2-15-2016-00017
GINOP
NKFIH-K 116263
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Intézményi repozitóriumban (DEA) tárolt változat
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3.

001-es BibID:BIBFORM083125
035-os BibID:(WoS)000508387300005 (Scopus)85074228284
Első szerző:Járvás Gábor (vegyészmérnök)
Cím:Practical sample pretreatment techniques coupled with capillary electrophoresis for real samples in complex matrices / Jarvas Gabor, Guttman Andras, Miekus Natalia, Baczek Tomasz, Jeong Sunkyung, Chung Doo Soo, Pätoprsty Vladimir, Masár Marián, Hutta Milan, Datinská Vladimira, Foret Frantisek
Dátum:2020
ISSN:0165-9936
Megjegyzések:By coupling a sample pretreatment technique of sample clean up and enrichment power with capillary electrophoresis (CE) of high-performance separation, the task of analyzing trace analytes in a complex matrix such as a biological sample can be carried out successfully with ease. This review aims for providing an overview of strategies to couple sample pretreatment techniques with capillary and related microscale (e.g., microchip) electrophoresis, practically adoptable in an automatic manner, without requiring serious modification of existing instruments to install sophisticated interfaces. In-line sample pretreatment techniques based on liquid phase microextraction performed before sample injection and on-line sample preconcentration techniques performed during or after sample injection are discussed with emphasis on the applicability to samples of high conductivity, commonly encountered for biological samples. An overview of the recent developments in microfluidic immobilized enzymatic microreactors which fit excellently to microchip CE is also given.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Trac-Trends In Analytical Chemistry. - 122 (2020), p. 2-9. -
További szerzők:Guttman András (1954-) (vegyészmérnök) Miȩkus, Natalia Bączek, Tomasz Jeong, Sunkyung Chung, Doo Soo Pätoprstý, Vladimir Masár Marián Hutta, Milan Datinská, Vladimira Foret, František
Pályázati támogatás:Bionano_GINOP-2.3.2-15-2016-00017
GINOP
K116263
NKFIH
NN127062
NKFIH
2018-2.1.17-TET-KR-2018-00010
NKFIH
ÚNKP-19-4
Egyéb
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Intézményi repozitóriumban (DEA) tárolt változat
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4.

001-es BibID:BIBFORM111411
035-os BibID:(cikkazonosító)117058 (WoS)000986990900001 (Scopus)85152634603
Első szerző:Jeong, Sunkyung
Cím:In-line microextraction techniques to improve the sensitivity and selectivity of capillary electrophoresis using commercial instruments / Sunkyung Jeong, Laszlo Hajba, Andras Guttman, Jiwoong Seol, Doo Soo Chung
Dátum:2023
ISSN:0165-9936
Megjegyzések:Capillary electrophoresis (CE) handles complex samples with excellent resolution, but has poor sensitivity because of the small detection volume and suffers from destacking of high-conductivity samples; therefore, sample preparation is often required for matrix cleanup and analyte enrichment. This review discusses operationally-simple sample preparation schemes which are easily adoptable by researchers using commercial CE instruments, wherein various solid-phase microextraction (SPME) and liquid-phase microextraction (LPME) techniques are ♭in-line' coupled (i.e., integrated) to the separation capillary without modifying the commercial CE instrument with sophisticated interfaces. In-line coupling refers to scenarios where the prepared sample is injected directly into the separation capillary. Then, sample loss is reduced and the enrichment factors can be significantly increased as the acceptor volume can be reduced to the nanoliter level. Cases involving subsequent on-line preconcentration are also discussed. In-line SPME-CE and LPME-CE are powerful tools for analyzing various samples, especially trace substances in complex biological matrices.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Capillary electrophoresis
Sample pretreatment
Solid-phase microextraction
Liquid-phase microextractionIn-line coupling
On-line preconcentration
Megjelenés:Trac-Trends In Analytical Chemistry. - 163 (2023), p. 1-14. -
További szerzők:Hajba László Guttman András (1954-) (vegyészmérnök) Seol, Jiwoong Chung, Doo Soo
Pályázati támogatás:2018-2.1.17-TÉT-KR-2018-00010,
Egyéb
2019-2.1.11-TÉT-2019-00068
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Intézményi repozitóriumban (DEA) tárolt változat
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5.

001-es BibID:BIBFORM099696
035-os BibID:(cikkazonosító)116407 (WoS)000712330500010 (Scopus)85114123547
Első szerző:Kaur, Harleen
Cím:Capillary electrophoresis and the biopharmaceutical industry : therapeutic protein analysis and characterization / Kaur Harleen, Beckman Jeff, Zhang Yiting, Li Zheng Jian, Szigeti Marton, Guttman Andras
Dátum:2021
ISSN:0165-9936
Megjegyzések:Capillary electrophoresis (CE) has emerged as a powerful technique for comprehensive physicochemical characterization of monoclonal antibodies (mAbs) as well as other therapeutic modalities. The method provides high resolution separation and high sensitivity characterization for analysis of therapeutic biomolecules. CE based techniques such as sodium dodecyl sulphate capillary gel electrophoresis (SDSCGE, also referred to as CE SDS), capillary zone electrophoresis (CZE) and imaged capillary isoelectric focusing (iCIEF) have been increasingly adopted to assess size heterogeneity, glycosylation heterogeneity and charge heterogeneity in mAbs and related therapeutic modalities. This paper reviews the latest application developments of CE based methods for routine release testing, stability testing and in-depth characterization. In addition, advantages and disadvantages of each of these techniques are critically discussed.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Capillary electrophoresis
Size heterogeneity
Charge variants
Glycosylation
Monoclonal antibodies
Therapeutic modalities
Biopharmaceuticals
Megjelenés:Trac-Trends In Analytical Chemistry. - 144 (2021), p. 1-10. -
További szerzők:Beckman, Jeff Zhang, Yiting Li, Zheng Jian Szigeti Márton (1986-) (környezetmérnök) Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:TKP2020-IKA-07
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Intézményi repozitóriumban (DEA) tárolt változat
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6.

001-es BibID:BIBFORM050956
Első szerző:Monzo, Alex
Cím:Proteolytic enzyme-immobilization techniques for MS-based protein analysis / Alex Monzo, Edit Sperling, András Guttman
Dátum:2009
ISSN:0165-9936
Megjegyzések:Protein digestion utilizing proteases (e.g., trypsin, Lys C and other proteolytic enzymes) is one of the key sample-preparation steps in contemporary proteomics, followed by liquid chromatography coupled to mass spectrometry (MS). Tryptic digestion is traditionally performed in aqueous solutions, usually applying the enzyme and the sample in a 50:1 protein-to-protease ratio. Long digestion times (up to 24 h), auto-digestion sub-products and poor enzyme-to-substrate ratio are common issues with liquid-phase protein-digestion processes. The use of enzymes immobilized onto solid supports can minimize these problems by increasing enzyme-to-substrate ratios, significantly speeding up digestion times and reducing autolysis. The other main goal of protease immobilization is to obtain rugged, efficient enzyme reactors.In this article, we review the most important proteolytic enzyme-immobilization techniques with the main emphasis on fabrication of trypsin microreactors and nanoreactors and their utilization in bottom-up proteomics. We also discuss data reportedly obtained using the various immobilization protocols with respect to enzyme activity and MS-sequence coverage.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Enzyme immobilization
Mass spectrometry
Protease
Protein analysis
Protein digestion
Proteolytic enzyme
Proteomics
Trypsin microreactor
Trypsin nanoreactor
Tryptic digestion
Megjelenés:Trac-Trends in Analytical Chemistry. - 28 : 7 (2009), p. 854-864. -
További szerzők:Sperling Edit Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:TéT A-10/2006
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7.

001-es BibID:BIBFORM115946
035-os BibID:(cikkazonosító)117397 (scopus)85175539890
Első szerző:Rathore, Anurag S.
Cím:Recent progress in high-throughput and automated characterization of N-glycans in monoclonal antibodies / Rathore Anurag S., Guttman Andras, Shrivastava Anuj, Joshi Srishti
Dátum:2023
ISSN:0165-9936
Megjegyzések:N-glycosylation of monoclonal antibody therapeutics is a post-translation modification and a critical quality attribute because of its significant impact on the bioavailability as well as the efficacy of these products. The structural complexity and heterogeneity of the asparagine linked oligosaccharides on monoclonal antibodies present a challenge towards their characterization. In order to control and monitor these N-glycosylations during commercial manufacturing of biotherapeutics, there is a continuous need for rapid, sensitive, robust, and affordable characterisation strategies. In this review, our primary focus is on recent advancements in high- throughput and automated techniques for sample preparation, data acquisition and analysis of monoclonal antibody N-glycans since 2015. This includes characterization at the intact glycoprotein, middle up, glycopeptide, and released glycan levels with the use of high-throughput and automated techniques. Bioinformatic tools have also been conferred including various databases, data analysis softwares, and computational tools for glycan structure builders.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
N-Glycosylation
IgG
Biosimilars
Critical quality attributes
Automation
High throughput
Bioinformatics
Megjelenés:Trac-Trends In Analytical Chemistry. - 169 (2023), p. 1-19. -
További szerzők:Guttman András (1954-) (vegyészmérnök) Shrivastava, Anuj Joshi, Srishti
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8.

001-es BibID:BIBFORM083126
035-os BibID:(WoS)000508387300020 (Scopus)85075579456
Első szerző:Szekrényes Ákos (vegyészmérnök)
Cím:Quantitative comparison of the N-glycosylation of therapeutic glycoproteins using the Glycosimilarity Index. A tutorial / Szekrenyes Akos, Szigeti Marton, Dvorakova Veronika, Jarvas Gabor, Guttman Andras
Dátum:2020
ISSN:0165-9936
Megjegyzések:Glycosylation is considered as one of the crucial critical quality attributes of therapeutic glycoproteins and for their biosimilar counterparts. Carbohydrate moieties of such biopharmaceuticals should be closely monitored during all stages of development and manufacturing and studied accordingly during comparability or similarity exercises. In therapeutic glycoprotein production, the batch-to-batch alteration in glycosylation represents an excellent indicator of process robustness. Due to the complexity of the obtained glycoanalytical profile it is challenging to determine and describe the level of similarity between the N-glycosylation characteristics of two glycoprotein production lots or between the reference batch and its biosimilar versions. In this tutorial, we provide a step-by-step approach to calculate a numerical similarity value of N-glycosylation, referred to as Glycosimilarity Index that can be efficiently used to assess the conformity degree of any new N-glycosylation profile to a given target profile.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Trac-Trends In Analytical Chemistry. - 122 (2020), p. 1-8. -
További szerzők:Szigeti Márton (1986-) (környezetmérnök) Dvorakova, Veronika Járvás Gábor (1982-) (vegyészmérnök) Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:BIONANO_GINOP-2.3.2-15-2016-00017
GINOP
K116263
NKFIH
NN127062
NKFIH
2018-2.1.17-TET-KR-2018-00010
NKFIH
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
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