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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:	BIBFORM065041
Első szerző:	Székely Andrea
Cím:	Multi Capillary SDS-Gel Electrophoresis for the Analysis of Fluorescently Labeled mAb preparations: a high throughput quality control process for the production of QuantiPlasma and PlasmaScan mAb libraries / Andrea Székely, Ákos Szekrényes, Márta Kerékgyártó, Attila Balogh, János Kádas, József Lázár, András Guttman, István Kurucz, László Takács
Dátum:	2014
ISSN:	0173-0835
Megjegyzések:	Molecular heterogeneity of mAb preparations is the result of various co- and post-translational modifications and to contaminants related to the production process. Changes in molecular composition results in alterations of functional performance, therefore quality control and validation of therapeutic or diagnostic protein products is essential. A special case is the consistent production of mAb libraries (QuantiPlasma? and PlasmaScan?) for proteome profiling, quality control of which represents a challenge because of high number of mAbs (>1000). Here, we devise a generally applicable multicapillary SDS-gel electrophoresis process for the analysis of fluorescently labeled mAb preparations for the high throughput quality control of mAbs of the QuantiPlasma? and PlasmaScan? libraries.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban capillary electrophoresis glycoform mAb proteomics quality control SDS
Megjelenés:	Electrophoresis. - 35 : 15 (2014), p. 2155-2162. -
További szerzők:	Szekrényes Ákos (1983-) (vegyészmérnök) Kerékgyártó Márta (1987-) (molekuláris biológus) Balogh Attila Kádas János (1976-) (molekuláris biológus, biokémikus, kertészmérnök) Lázár József Guttman András (1954-) (vegyészmérnök) Kurucz István Takács László (1955-)
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM043657
Első szerző:	Váradi Csaba (molekuláris biológus)
Cím:	Analysis of Haptoglobin N-glycome Alterations in Inflammatory and Malignant Lung Diseases by Capillary Electrophoresis / Cs. Varadi, S. Mittermayr, A. Szekrenyes, J. Kadas, L. Takacs, I. Kurucz, A. Guttman
Dátum:	2013
ISSN:	0173-0835
Megjegyzések:	A capillary electrophoresis based method was introduced to compare the N-glycosylation profile ofhaptoglobin in normal and pathologic conditions. To assess the biomarker potential of glycosylationchanges in various lung diseases, haptoglobin was isolated from plasma samples of healthy, pneumonia,chronic obstructive pulmonary disease (COPD) and lung cancer patients by means of two haptoglobinspecific monoclonal antibodies. Haptoglobin N-glycans were then enzymatically released, fluorescentlylabeled and profiled by capillary electrophoresis. Disease associated changes of core and antennaryfucosylation were identified by targeted exoglycosidase digestions and their levels were compared inthe different patient groups. Terms such as of core- and arm-fucosylation degree, as well as branchingdegreewere introduced for easier characterization of the changes and statistical analysis was used toexamine which structures are responsible for the observed differences. Increased level of ?1-6fucosylated tri-antennary glycans was found in all disease groups compared to the control. Elevatedamounts of core- and arm fucosylation on tetra-antennary glycans were detected in the lung cancergroup compared to the COPD group. A larger scale study is necessary to confirm and validate thesepreliminary findings in the glycosylation changes of haptoglobin, so could then be used as biomarkers inthe diagnosis of malignant and inflammatory lung diseases.
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban biomarker capillary electrophoresis
Megjelenés:	Electrophoresis. - 34 : 16 (2013), p. 2287-2294. -
További szerzők:	Mittermayr, Stefan (1983-) (bioinformatikus) Szekrényes Ákos (1983-) (vegyészmérnök) Kádas János (1976-) (molekuláris biológus, biokémikus, kertészmérnök) Takács László (1955-) Kurucz István Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:	K-81839 OTKA
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat DOI
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