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001-es BibID:	BIBFORM134721
Első szerző:	Guttman András (vegyészmérnök)
Cím:	Capillary Gradient Gel Electrophoresis / Guttman Andras, Auer Felicia
Dátum:	2025
ISSN:	2310-2861
Megjegyzések:	In the last half-century, capillary gel electrophoresis (CGE) became a versatile and high-performance analytical platform for the separation of complex biomolecular mixtures featuring rapid separations, high efficiency, and small sample consumption. Integrating a pore-size gradient mechanism in CGE makes it possible to achieve enhanced selectivity of polyionic macromolecules such as SDS-proteins and nucleic acids. This review provides a comprehensive overview of the theoretical foundations and operational principles of capillary pore-size gradient gel electrophoresis (CGGE), including the physicochemical basis of gradient formation, the influence of pore-size distributions on analyte mobility, and the challenges of generating stable, reproducible gradients in narrow-bore capillaries. Instrumental considerations such as capillary surface treatment, gradient filling and polymerization strategies, temperature and voltage control, detection modalities, and method-development frameworks are discussed in detail, emphasizing their critical impact on analytical performance and reproducibility. Key application areas in bioanalytical chemistry are highlighted, covering nucleic acid analysis and peptide/protein characterization. CGGE offers unique analytical advantages where fine molecular discrimination, tunable selectivity, and high resolution in a broad molecular weight range are required.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk capillary electrophoresis pore-size gradient gel sieving matrices proteins nucleic acids
Megjelenés:	Gels. - 12 : 1 (2025), p. 1-15. -
További szerzők:	Auer, Felicia
Pályázati támogatás:	PTP2025 Egyéb 2023-1.2.1-ERA_NET-2023-00012 Egyéb 2025-2.1.1-EKÖP Egyéb ADVANCED_150780 Egyéb
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001-es BibID:	BIBFORM126136
035-os BibID:	(Scopus)85213374930 (WoS)001383935400001
Első szerző:	Sárközy Dániel (PhD hallgató)
Cím:	Activation Energy of SDS-Protein Complexes in Capillary Electrophoresis with Tetrahydroxyborate Cross-Linked Agarose Gels / Sárközy Dániel, Guttman, András
Dátum:	2024
ISSN:	2310-2861
Megjegyzések:	Hydrogels like agarose have long been used as sieving media for the electrophoresis-based analysis of biopolymers. During gelation, the individual agarose strands tend to form hydrogen-bond mediated double-helical structures, allowing thermal reversibility and adjustable pore sizes for molecular sieving applications. The addition of tetrahydroxyborate to the agarose matrix results in transitional chemical cross-linking, offering an additional pore size adjusting option. Separation of SDS-proteins during gel electrophoresis is an activated process defined by the interplay between viscosity, gelation/cross-link formation/distortion, and sample conformation. In this paper, the subunits of a therapeutic monoclonal antibody were separated by capillary SDS agarose gel electrophoresis at different temperatures. The viscosity of the separation matrix was also measured at all temperatures. In both instances, Arrhenius plots were used to obtain the activation energy values. It was counterintuitively found that larger SDS?protein complexes required lower activation energies while their low-molecular-weight counterparts needed higher activation energy for their electromigration through the sieving matrix. As a first approximation, we considered this phenomenon the result of the electric force-driven distortion of the millisecond range lifetime reticulations by the larger and consequently more heavily charged electromigrating molecules. In the meantime, the sieving properties of the gel were still maintained, i.e., they allowed for the size-based separation of the sample components, proving the existence of the reticulations. Information about the activation energy sheds light on the possible deformation of the sieving matrix and the solute molecules. In addition, the activation energy requirement study helped in optimizing the separation temperature, e.g., with our sample mixture, the highest resolution was obtained for the high-molecular-weight fragments, i.e., between the non-glycosylated heavy chain and heavy-chain subunits at 25 ?C (lower Ea requirement), while 55 ?C was optimal for the lower-molecular-weight light chain and non-glycosylated heavy chain pair (lower Ea requirement). Future research directions and possible applications are also proposed.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk agarose gel temperature activation energy SDS-protein complexes capillary electrophoresis
Megjelenés:	Gels. - 10 : 12 (2024), p. 1-13. -
További szerzők:	Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:	DE Publikációs Tudománytámogatási Program Egyéb 2023-1.2.1-ERA_NET-2023-00015 Egyéb
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001-es BibID:	BIBFORM100010
035-os BibID:	(WoS)000967943600001 (Scopus)85123776256
Első szerző:	Sárközy Dániel (PhD hallgató)
Cím:	Capillary Sodium Dodecyl Sulfate Agarose Gel Electrophoresis of Proteins / Daniel Sarkozy, Andras Guttman
Dátum:	2022
ISSN:	2310-2861
Tárgyszavak:	Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk
Megjelenés:	Gels. - 8 : 2 (2022), p. 1-10. -
További szerzők:	Guttman András (1954-) (vegyészmérnök)
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