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1.

001-es BibID:BIBFORM113960
035-os BibID:(WoS)001043559400001 (Scopus)85166981215
Első szerző:Auer, Felicia
Cím:Size separation of sodium dodecyl sulfate-proteins by capillary electrophoresis in dilute and ultra-dilute dextran solutions / Felicia Auer, Andras Guttman
Dátum:2023
ISSN:0173-0835 1522-2683
Megjegyzések:SDS capillary gel electrophoresis is a widely used in the biopharma and the biomedical fields for rapid size separation of proteins. However, very limited information is available on the use of dilute and ultra-dilute sieving matrices for SDS?protein analysis. Here, background electrolytes (BGEs) containing 1%? 0% dextran were used in borate-based BGE to separate a protein sizing ladder (PSL) ?225 kDa and the intact and subunit forms of a therapeutic monoclonal antibody (mAb). The separation performance for the PSL and mAb components differed significantly with decreasing dextran concentration. Ferguson and reptation plots were used to elucidate the separation mechanism. Highly diluted dextran solutions resulted in linear Ferguson plots for both solute types (cf. Ogston theory) in spite of this model assumes a rigid pore structure, thus cannot describe the separation mechanism in ultra-dilute polymer solutions with no reticulations. The saddle differences between the resolution of the PSL and the intact/subunit mAb forms in ultra-dilute dextran-borate matrices suggested the importance of shape selectivity, manifested by the adequate separation of the SDS covered intact as well as light and heavy chain subunits of the therapeutic mAb even at zero dextran concentration.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
borate
capillary gel electrophoresis
dextran
SDS-proteins
ultra-dilute polymer
Megjelenés:Electrophoresis. - 44 : 19-20 (2023), p. 1607-1614. -
További szerzők:Guttman András (1954-) (vegyészmérnök)
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2.

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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3.

001-es BibID:BIBFORM083095
035-os BibID:(Scopus)85073965631 (WOS)000488353700001
Első szerző:Döncző Boglárka (biológiatanár-földrajztanár)
Cím:Effect of the elapsed time between sampling and formalin fixation on the N-glycosylation profile of mouse tissue specimens / Donczo Boglarka, Kiraly Gabor, Guttman Andras
Dátum:2019
ISSN:0173-0835 1522-2683
Megjegyzések:Formalin-fixed, paraffin-embedded (FFPE) samples are generally used for histology-study, however, they also possess importantmolecular diagnostics information. While it has been reported that the N-glycan moieties of glycoproteins is not affected by the FFPE process, no information is available about the effect of the elapsed time between sampling and fixation on the resulting N-glycosylation profile. In this study, lung, brain, heart, spleen, liver, kidney, and intestine mouse tissue specimens were used for N-glycan profiling analysis and the elapsed sampling time effect was investigated with the lung tissue. N-glycan extraction from the tissue samples was performed by glycoprotein retrieval from the FFPE specimens using radioimmunoprecipitation assay (RIPA) buffer followed PNGase F digestion. The released oligosaccharides were fluorophore labeled and analyzed by capillary electrophoresis-laser induced fluorescent detection (CE-LIF). N-glycosylation profiles of freshly collected lung-tissue samples (zero time point), as well as 1 and 2 h after sampling were compared by carbohydrate profiling and exoglycosidase treatment based deep glycomic analysis. It was found that up to two hours of room temperature storage of tissue specimens apparently did not cause changes in the N-glycosylation profiles of complex carbohydrates, but resulted in considerable decrease in the amount of linear glucose oligomers and high mannose type glycans present in the samples.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Electrophoresis. - 40 : 23-24 (2019), p. 3057-3061. -
További szerzők:Király Gábor (1988-) (biológus) Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:K 116263
NKFIH
BIONANO_GINOP-2.3.2-15-2016-00017
GINOP
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4.

001-es BibID:BIBFORM071240
035-os BibID:(Scopus)85016329810 (WOS)000403912000008
Első szerző:Döncző Boglárka (biológiatanár-földrajztanár)
Cím:Molecular glycopathology by capillary electrophoresis : analysis of the N-glycome of formalin-fixed paraffin-embedded mouse tissue samples / Donczo Boglarka, Szarka Mate, Tovari Jozsef, Ostoros Gyorgyi, Csanky Eszter, Guttman Andras
Dátum:2017
ISSN:0173-0835
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Electrophoresis. - 38 : 12 (2017), p. 1602-1608. -
További szerzők:Szarka Máté (1990-) Tóvári József Ostoros Györgyi Csánky Eszter (1959-) (tüdőgyógyász, klinikai immunológus, allergológus) Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:K116263
NKFIH
116295
NKFIH
BIONANO_GINOP-2.3.2-15-2016-00017
GINOP
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5.

001-es BibID:BIBFORM070702
035-os BibID:(Scopus)84987660600 (WOS)000383596800002
Első szerző:Döncző Boglárka (biológiatanár-földrajztanár)
Cím:N-Glycosylation analysis of formalin fixed paraffin embedded samples by capillary electrophoresis / Donczo Boglarka, Szigeti Marton, Ostoros Gyorgyi, Gacs Alexandra, Tovari Jozsef, Guttman Andras
Dátum:2016
ISSN:0173-0835
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Electrophoresis. - 37 : 17-18 (2016), p. 2292-2296. -
További szerzők:Szigeti Márton (1986-) (környezetmérnök) Ostoros Györgyi Gács Alexandra Tóvári József Guttman András (1954-) (vegyészmérnök)
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6.

001-es BibID:BIBFORM050950
Első szerző:Garrido-Medina, Raúl
Cím:Analysis of alpha-1-acid glycoprotein isoforms using CE-LIF with fluorescent thiol derivatization / Raúl Garrido-Medina, Angel Puerta, Zuly Rivera-Monroy, Mercedes de Frutos, Andras Guttman, José Carlos Diez-Masa
Dátum:2012
ISSN:0173-0835
Megjegyzések:The analysis of glycoprotein isoforms is of high interest in the biomedical field and clinical chemistry. Many studies have demonstrated that some glycoprotein isoforms could serve as biomarkers for several major diseases, such as cancers and vascular diseases, among others. Capillary zone electrophoresis (CZE) is a well-established technique to separate glycoprotein isoforms, however, it suffers from limited sensitivity when UV-Vis detection is used. On the other hand, with laser-induced fluorescence (LIF) detection, derivatization reaction to render the proteins fluorescent can destroy the resolution of the isoforms. In this work, a derivatization procedure through the thiol groups of glycoproteins using either 5-(iodoacetamide) fluorescein (5-IAF) or BODIPY iodoacetamide is presented with the model protein of alpha-1-acid glycoprotein (AGP). The derivatization process presented enabled high-resolution analysis of AGP isoforms by CZE-LIF. The derivatization procedure was successfully applied to label AGP from samples of serum and secretome of artery tissue, enabling the separation of the AGP isoforms by CE-LIF in natural samples at different concentration levels.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
AGP-isoforms
BODIPY
CZE
Fluorescein
LIF-detection
Megjelenés:Electrophoresis. - 33 : 7 (2012), p. 1113-1119. -
További szerzők:Puerta, Angel Rivera-Monroy, Zuly Frutos, Mercedes de Guttman András (1954-) (vegyészmérnök) Diez-Masa, José Carlos
Pályázati támogatás:K-81839
OTKA
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7.

001-es BibID:BIBFORM099586
Első szerző:Guttman András (vegyészmérnök)
Cím:Biomarker discovery and related topics / Andras Guttman
Dátum:2011
ISSN:0173-0835 1522-2683
Tárgyszavak:Természettudományok Kémiai tudományok szerkesztői levél
folyóiratcikk
Megjelenés:Electrophoresis. - 32 : 15 (2011), p. 1915. -
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8.

001-es BibID:BIBFORM077848
035-os BibID:(PMID)30101988 (Scopus)85052790800 (WOS)000450406900003
Első szerző:Guttman András (vegyészmérnök)
Cím:Authors' Reply to the Commentary in the journal of Electrophoresis regarding "The effect of simulated space radiation on the N-glycosylation of human immunoglobulin G1" by J.J. Bevelacqua and S.M.J. Mortazavi / Andras Guttman, Szabolcs Szilasi, Boglarka Donczo, Mate Szarka
Dátum:2018
ISSN:0173-0835 1522-2683
Megjegyzések:By reading the commentary of Bevelacqua and Mortazavi regarding our recently published paper titled as "The effect of simulated space radiation on the N?glycosylation of human immunoglobulin G1"[1], we are afraid that some of the important messaging aspects of our paper might not have been articulated adequately to be fully understandable for a wider audience, i.e., not separation scientists. First, we should clarify that complete space radiation description was not the goal of this paper. In this short communication we only intended to show the effect of simulated space radiation on the conserved N?glycosylation of IgG1 molecules with the goal to understand if they could be utilized as disease biomarkers during longer space missions, similar to that as they are currently used here on Earth, e.g. for autoimmune disease or aging markers. Therefore, no discussion was given about any biological effects either as our study only investigated the qualitative effects of proton irradiation on the N?linked carbohydrate decomposition of IgG type 1 molecules with the intent of suggesting them to be used as biomarkers during deep space travel. Radioadaptation was never an issue in our study for the reasons mentioned above.
Tárgyszavak:Orvostudományok Elméleti orvostudományok szerkesztői levél
folyóiratcikk
Glycans
IgG
Space
Megjelenés:Electrophoresis. - 39 : 22 (2018), p. 2851-2853. -
További szerzők:Szilasi Szabolcs Döncző Boglárka (1987-) (biológiatanár-földrajztanár) Szarka Máté (1990-)
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9.

001-es BibID:BIBFORM050952
Első szerző:Guttman András (vegyészmérnök)
Cím:Haplotyping of putative microRNA-binding sites in the SNAP-25 gene / Reka Kovacs-Nagy, Peter Sarkozy, Jimmy Hu, Andras Guttman, Maria Sasvari-Szekely, Zsolt Ronai
Dátum:2011
ISSN:0173-0835
Megjegyzések:Synaptosomal-associated protein 25 (SNAP-25) plays a crucial role in exocitosis. Single nucleotide polymorphisms (rs3746544 and rs1051312) in the 3· un-translated region of the SNAP-25 gene have been described to be in association with attention-deficit hyperactivity disorder. As the disease affects millions of children world-wide, understanding the genetic background of attention-deficit hyperactivity disorder is of crucial importance. Efficient and reliable PCR-RFLP protocols were elaborated for the genotyping of the rs3746544 and rs1051312 SNPs employing a high-throughput capillary electrophoresis method for fragment analysis. A novel real-time PCR-based technique was used applying sequence specific TaqMan probes to haplotype the two SNPs, and the G?C haplotype could not be detected in a large Caucasian population (N=1376). These findings have been confirmed by molecular biology tools as well as by the PHASE Bayesian computational approach. In silico analyses have suggested that the two SNPs might alter microRNA binding and thus have an effect on SNAP-25 production. We have demonstrated that this biological information can be revealed only by direct haplotype analysis emphasizing the importance of our novel molecular haplotye analysis protocol. Results of the study of the two SNPs might shed light on the association of SNAP-25 variants and pathological phenotypes at the molecular level.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Haplotype
miRSNP
Real-time PCR
Synaptosomal-associated protein 25
Megjelenés:Electrophoresis. - 32 : 15 (2011), p. 2013-2020. -
További szerzők:Kovács-Nagy Réka Sárközy Péter Hu, Jimmy Guttman András (1954-) (vegyészmérnök) Sasvári-Székely Mária Rónai Zsolt
Pályázati támogatás:NKTH TECH-08-A1/2-2008-0120
Egyéb
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10.

001-es BibID:BIBFORM058347
Első szerző:Guttmann Miklós
Cím:Comparative glycoprofiling of HIV gp120 immunogens by capillary electrophoresis and MALDI mass spectrometry / Miklós Guttman, Csaba Váradi, Kelly K. Lee, András Guttman
Dátum:2015
ISSN:0173-0835
Megjegyzések:The Human Immunodeficiency Virus (HIV) envelope glycoprotein (Env) is the primary antigenic feature on the surface of the virus and is of key importance in HIV vaccinology. Vaccine trials with the gp120 subunit of Env are ongoing with the recent RV144 trial showing moderate efficacy. gp120 is densely covered with N-linked glycans that are thought to help evade the host's humoral immune response. To assess how the global glycosylation patterns vary between gp120 constructs, the glycan profiles of several gp120s were examined by capillary electrophoresis with laser induced fluorescence detection and MALDI-MS. The glycosylation profiles were found to be similar for chronic vs. transmitter/founder isolates and only varied moderately between gp120s from different clades. This study revealed that the addition of specific tags, such as the gD tag used in the RV144 trial, had significant effects on the overall glycosylation patterns. Such effects are likely to influence the immunogenicity of various Env immunogens and should be considered for future vaccine strategies, emphasizing the importance of the glycosylation analysis approach described in this paper.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
HIV glycosylation
Megjelenés:Electrophoresis 36 : 11-12 (2015), p. 1305-1313. -
További szerzők:Váradi Csaba (1988-) (molekuláris biológus) Lee, Kelly K. Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:NIH F32-GM097805
Egyéb
Internet cím:DOI
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11.

001-es BibID:BIBFORM106817
035-os BibID:(scopus)85129736585 (wos)000787278500001
Első szerző:He, Xiaoping
Cím:Evaluation of an icIEF-MS system for comparable charge variant analysis of biotherapeutics with rapid peak identification by mass spectrometry / He Xiaoping, ElNaggar Mariam, Ostrowski Maggie A., Guttman Andras, Gentalen Erik, Sperry Justin
Dátum:2022
ISSN:0173-0835 1522-2683
Megjegyzések:Protein therapeutics are usually produced in heterogeneous forms during bioproduction and bioprocessing. Heterogeneity results from post-translational modifications that can yield charge variants and require characterization throughout product development and manufacturing. Isoelectric focusing (IEF) with UV detection is one of the most common methods to evaluate protein charge heterogeneity in the biopharmaceutical industry. To identify charge variant peaks, a new imaged microfluidic chip-based isoelectric focusing (icIEF) system coupled directly to mass spectrometry was recently reported. Bridging is required to demonstrate comparability between existing and new technology. As such, here we demonstrate the comparability of the pI value measurement and relative charge species distributions between the icIEF-MS system and the control data from a frequently utilized methodology in the biopharmaceutical industry for several blinded development-phase biopharmaceutical monoclonal antibodies across a wide pI range of 7.3-9.0. Hyphenation of the icIEF system with mass spectrometry enabled direct and detailed structural determination of a test molecule, with masses suggesting acidic and basic shifts are caused by sialic acid additions and the presence of unprocessed lysine residues. In addition, MS analysis further identified several low-abundance glycoforms. The icIEF-MS system provides sample quantification, characterization, and identification of mAb proteoforms without sacrificing icIEF quantification comparability or speed.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Electrophoresis. - 43 : 11 (2022), p. 1215-1222. -
További szerzők:ElNaggar, Mariam Ostrowski, Maggie A. Guttman András (1954-) (vegyészmérnök) Gentalen, Erik Sperry, Justin
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12.

001-es BibID:BIBFORM083086
035-os BibID:(Scopus)85067395975 (WOS)000490455400004
Első szerző:Járvás Gábor (vegyészmérnök)
Cím:Commentary regarding "Decision support algorithm for the selection of analytical methods in organic compounds detection for future extraterrestrial exploratory missions" / Járvás Gábor, Guttman András
Dátum:2019
ISSN:0173-0835 1522-2683
Megjegyzések:M?aty?as et al. recently published their paper entitled as "Decision support algorithm for the selection of analytical methods in organic compounds detection for future extraterrestrial exploratory missions," which we found interesting. However, there are some points of the developed method that need to be refined to get a practical tool for practitioners. In this commentary, we have summarized our suggestions and comments mainly from the chemical/separation point of view.
Tárgyszavak:Orvostudományok Elméleti orvostudományok hozzászólás
folyóiratcikk
Megjelenés:Electrophoresis. - 40 : 20 (2019), p. 2662-2663. -
További szerzők:Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:K 116263
NKFIH
NN 127062
NKFIH
BIONANO GINOP-2.3.2-15-2016-00017
GINOP
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