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001-es BibID:	BIBFORM099692
035-os BibID:	(WOS)000755261400008 (Scopus)85117105756
Első szerző:	Kun Renáta (biotechnológus)
Cím:	Capillary Electrophoresis-Based N-Glycosylation Analysis in the Biomedical and Biopharmaceutical Fields / Renata Kun, Eszter Jóna, Andras Guttman
Dátum:	2021
ISSN:	0065-2598
Megjegyzések:	Glycomics has a growing interest in the biopharmaceutical industry and biomedical research requiring new high-performance and high-sensitivity bioanalytical tools. Analysis of N-glycosylation is very important during the development of protein therapeutics and it also plays a key role in biomarker discovery. The most frequently used glycoanalytical methods are capillary electrophoresis, liquid chromatography, and mass spectrometry. In this chapter, the capillary electrophoresis-based N-linked carbohydrate analysis methods are conferred with emphasis on its use in the biopharmaceutical and biomedical fields.
ISBN:	978-3-030-77251-2 978-3-030-77254-3
Tárgyszavak:	Orvostudományok Elméleti orvostudományok könyvfejezet könyvrészlet Capillary electrophoresis N-glycans Biopharmaceuticals Biomarkers
Megjelenés:	Separation Techniques Applied to Omics Sciences / Ed. Ana Valéria Colnaghi Simionato. - p. 129-137. -
További szerzők:	Jóna Eszter Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:	OTKA-116263 OTKA NN127062 OTKA 2018-2.1.17-TÉT-KR-2018-00010 Egyéb BIONANO_GINOP-2.3.2-15-2016- 00017 GINOP
Internet cím:	DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM106825
035-os BibID:	(cikkazonosító)8192 (scopus)85143597041 (wos)000896340300001
Első szerző:	Torok Rebeka
Cím:	The Effect of Sample Glucose Content on PNGase F-Mediated N-Glycan Release Analyzed by Capillary Electrophoresis / Torok Rebeka, Auer Felicia, Farsang Robert, Jona Eszter, Jarvas Gabor, Guttman Andras
Dátum:	2022
ISSN:	1420-3049
Megjegyzések:	Protein therapeutics have recently gained high importance in general health care along with applied clinical research. Therefore, it is important to understand the structure?function relationship of these new generation drugs. Asparagine-bound carbohydrates represent an important critical quality attribute of therapeutic glycoproteins, reportedly impacting the efficacy, immunogenicity, clearance rate, stability, solubility, pharmacokinetics and mode of action of the product. In most instances, these linked N-glycans are analyzed in their unconjugated form after endoglycosidase-mediated release, e.g., PNGase F-mediated liberation. In this paper, first, N-glycan release kinetics were evaluated using our previously reported in-house produced 6His-PNGase F enzyme. The resulting deglycosylation products were quantified by sodium dodecyl sulfate capillary gel electrophoresis to determine the optimal digestion time. Next, the effect of sample glucose content was investigated as a potential endoglycosidase activity modifier. A comparative Michaelis-Menten kinetics study was performed between the 6His-PNGase F and a frequently employed commercial PNGase F product with and without the presence of glucose in the digestion reaction mixture. It was found that 1 mg/mL glucose in the sample activated the 6His-PNGase F enzyme, while did not affect the release efficiency of the commercial PNGase F. Capillary isoelectric focusing revealed subtle charge heterogeneity differences between the two endoglycosidases, manifested by the lack of extra acidic charge variants in the cIEF trace of the 6His-PNGase F enzyme, which might have possibly influenced the glucose-mediated enzyme activity differences.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk
Megjelenés:	Molecules. - 27 : 23 (2022), p. 1-8. -
További szerzők:	Auer, Felicia Farsang Róbert Jóna Eszter Járvás Gábor (1982-) (vegyészmérnök) Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:	UNKP-22-3-I Egyéb
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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