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001-es BibID:	BIBFORM047874
035-os BibID:	PMID:21732557
Első szerző:	Kovács András László (biológus, biológia-kémia tanár)
Cím:	Fractionation of the human plasma proteome for monoclonal antibody proteomics-based biomarker discovery / András Kovács, Edit Sperling, József Lázár, Attila Balogh, János Kádas, Ákos Szekrényes, László Takács, István Kurucz, András Guttman
Dátum:	2011
ISSN:	0173-0835
Megjegyzések:	mAb proteomics, a reversed biomarker discovery approach, is a novel methodology to recognize the proteins of biomarker potential, but requires subsequent antigen identification steps. While in case of high-abundant proteins, it generally does not represent a problem, for medium or lower abundant proteins, the identification step requires a large amount of sample to assure the proper amount of antigen for the ID process. In this article, we report on the use of combined chromatographic and precipitation techniques to generate a large set of fractions representing the human plasma proteome, referred to as the Analyte Library, with the goal to use the relevant library fractions for antigen identification in conjunction with mAb proteomics. Starting from 500mL normal pooled human plasma, this process resulted in 783 fractions with the average protein concentration of 1mg/mL. First, the serum albumin and immunoglobulins were depleted followed by prefractionation by ammonium sulfate precipitation steps. Each precipitate was then separated by size exclusion chromatography, followed by cation and anion exchange chromatography. The 20 most concentrated ion exchange chromatography fractions were further separated by hydrophobic interaction chromatography. All chromatography and precipitation steps were carefully designed aiming to maintain the native forms of the intact proteins throughout the fractionation process. The separation route of vitamin D-binding protein (an antibody proteomics lead) was followed in all major fractionation levels by dot blot assay in order to identify the library fraction it accumulated in and the identity of the antigen was verified by Western blot.
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Electrophoresis. - 32 : 15 (2011), p. 1916-1925. -
További szerzők:	Sperling Edit Lázár József Balogh Attila (bőrgyógyász) Kádas János (1976-) (molekuláris biológus, biokémikus, kertészmérnök) Szekrényes Ákos (1983-) (vegyészmérnök) Takács László (1955-) Kurucz István Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:	K81839 OTKA TECH-09-A1-2009-0113; mABCHIC Egyéb
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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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 Egyéb
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM099310
035-os BibID:	(cikkazonosító)114483
Első szerző:	Szabó Miklós (tüdőgyógyász)
Cím:	N-glycosylation structure - function characterization of omalizumab, an anti-asthma biotherapeutic product / Miklos Szabo, Csenge Filep, Mate Nagy, Daniel Sarkozy, Marton Szigeti, Edit Sperling, Eszter Csanky, Andras Guttman
Dátum:	2022
ISSN:	0731-7085
Megjegyzések:	Omalizumab, a glycoprotein based biotherapeutics, is one of the most frequently used targeted antibody biopharmaceutical to reduce asthma exacerbations, improve lung function and reduce oral corticosteroid use. The effector function and clearance time of such glycoprotein drugs is affected by their N-glycosylation, that defines the required administration frequency to improve the quality of life in appropriately selected patients. Therefore, the glycosylation of biologics is an important critical quality attribute (CQA). The profile of asparagine linked carbohydrates is greatly dependent on the manufacturing process. Even a small deviation may have a major effect on the structure and therefore the function of the biotherapeutic product. For this reason, comprehensive N-glycosylation analysis is of high importance during production and release. Capillary electrophoresis (CE) is one of the frequently used tools to characterize protein therapeutics and utilized by the biopharmaceutical industry for protein and glycan level analysis, which are key parts both for drug development and quality control. To reveal important structure ? function relationships, characterization of omalizumab is presented using capillary SDS gel electrophoresis with UV detection at the protein level and capillary gel electrophoresis with laser induced fluorescent detection at the N-linked carbohydrate level. This latter technique was also used for oligosaccharide sequencing for glycan structure validation. The results suggested no ADCC function ? structure relationship due to the mostly core fucosylated biantennary glycans found. However, the presence of the high mannose structures probably affects the clearance rate of the drug.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk mAb karakterizálás kapilláris gélelektroforézis
Megjelenés:	Journal of Pharmaceutical and Biomedical Analysis. - 209 (2022), p. 1-5. -
További szerzők:	Filep Csenge Boróka (1993-) (biomérnök) Nagy Máté Sárközy Dániel (1993-) (PhD hallgató) Szigeti Márton (1986-) (környezetmérnök) Sperling Edit Csánky Eszter (1959-) (tüdőgyógyász, klinikai immunológus, allergológus) Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:	BIONANO_GINOP-2.3.2-15-2016-00017 GINOP NN 127062 NKFIH TKP2020-IKA-07 Egyéb 2020-4.1.1-TKP2020 Egyéb
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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