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001-es BibID:BIBFORM084562
035-os BibID:(Scopus)84961282078 (WOS)000379133500002
Első szerző:Bodnár Judit
Cím:Enzymatic removal of N-glycans by PNGase F coated magnetic microparticles / Bodnar Judit, Szekrenyes Akos, Szigeti Marton, Jarvas Gabor, Krenkova Jana, Foret Frantisek, Guttman Andras
Dátum:2016
ISSN:0173-0835 1522-2683
Megjegyzések:Investigation of protein glycosylation is an important area in biomarker discovery and biopharmaceutical research. Alterations in protein N-glycosylation can be an indication of changes in pathological conditions in the medical field or production parameters of biotherapeutics. Rapid development of these disciplines calls for fast, high-throughput, and reproducible methods to analyze protein N-glycosylation. Currently used methods require either long deglycosylation times or large excess of enzymes. In this paper, we report on the use of PNGase F immobilization onto the surface of magnetic microparticles and their use in rapid and efficient removal of N-glycans from glycoproteins. The use of immobilized PNGase F also allowed reusability of the enzyme-coated beads as the magnetic microparticles can be readily partitioned from the sample by a magnet after each deglycosylation reaction. The efficiency and activity of the PNGase F coated magnetic beads was compared with in-solution enzyme reactions using standard glycoproteins possessing the major N-glycan types of neutral, high mannose, and highly sialylated carbohydrates. The PNGase F coated magnetic beads offered comparable deglycosylation level to the conventional in-solution based method in 10-min reaction times for the model glycoproteins of immunoglobulin G (mostly neutral carbohydrates), ribonuclease B (high mannose type sugars), and fetuin (highly sialylated oligosaccharides) with the special features of easy removal of the enzyme from the reaction mixture and reusability.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Deglycosylation
Enzyme immobilization
Magnetic microparticles
PNGase F
Megjelenés:Electrophoresis. - 37 : 10 (2016), p. 1264-1269. -
További szerzők:Szekrényes Ákos (1983-) (vegyészmérnök) Szigeti Márton (1986-) (környezetmérnök) Járvás Gábor (1982-) (vegyészmérnök) Krenkova, Jana Foret, František Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:K116263
NKFIH
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2.

001-es BibID:BIBFORM085475
Első szerző:Járvás Gábor (vegyészmérnök)
Cím:Characterization of a Porous Nano-electrospray Capillary Emitter at Ultra-low Flow Rates / Jarvas Gabor, Fonslow Bryan, Yates John R., Foret Frantisek, Guttman Andras
Dátum:2017
ISSN:0021-9665
Megjegyzések:Biopharmaceuticals, especially therapeutic monoclonal antibodies, have emerged as a very promising new generation of protein-based drugs. However, their comprehensive analysis continues to pose new challenges for the bioanalytical field. Hyphenation of capillary electrophoresis with electrospray ionization (CE-MS) is a promising technique to address these challenges. One of the main advantages of CE-MS is the ability to produce stable electrospray at ultra-low flow rates (5?20 nl/min range). In this short communication we report on the characterization of a porous nanoelectrospray capillary emitter focusing on the effects of ultra-low flow rate on ionization efficiency, ion suppression and detection sensitivity. Ion suppression effect of a poorly-ionizable sugar in the presence of an easily-ionized peptide was reduced by almost 2-fold. Intact therapeutic antibody infusion analysis demonstrated that MS detection sensitivity increased by an order of magnitude with the decrease of flow rate from 250 nL/min to 20 nL/min using the nano-electrospray capillary emitter.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Journal Of Chromatographic Science. - 55 : 1 (2017), p. 47-51. -
További szerzők:Fonslow, Bryan Yates, John R. Foret, František Guttman András (1954-) (vegyészmérnök)
Internet cím:Szerző által megadott URL
DOI
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
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