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Book ; Online: Gas Chromatography : Biochemicals, Narcotics and Essential Oils

Salih, Bekir / Ç, r

2012

Keywords	Spectrum analysis, spectrochemistry, mass spectrometry ; Solid state chemistry
Size	1 electronic resource (250 pages)
Publisher	IntechOpen
Document type	Book ; Online
Note	English ; Open Access
HBZ-ID	HT021046666
ISBN	9789535149774 ; 9535149776
Database	ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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Book ; Online: Gas Chromatography in Plant Science, Wine Technology, Toxicology and Some Specific Applications

Salih, Bekir / Ç, r

2012

Keywords	Spectrum analysis, spectrochemistry, mass spectrometry
Language	English
Size	1 electronic resource (360 pages)
Publisher	IntechOpen
Document type	Book ; Online
Note	English
HBZ-ID	HT030646864
ISBN	9789535143413 ; 9535143417
Database	ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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Article ; Online: Site-specific N-glycosylation analysis of human thyroid thyroglobulin by mass spectrometry-based Glyco-analytical strategies.

Kayili, H Mehmet / Salih, Bekir

Journal of proteomics

2022 Volume 267, Page(s) 104700

Abstract: Human thyroglobulin (Tg), which has many glycosylation sites, is an essential protein produced by the human thyroid glands. Although human Tg N-glycans play critical roles in the cellular events of the Thyroid gland, the site-specific distribution of ... ...

Abstract	Human thyroglobulin (Tg), which has many glycosylation sites, is an essential protein produced by the human thyroid glands. Although human Tg N-glycans play critical roles in the cellular events of the Thyroid gland, the site-specific distribution of glycan structures has not been studied in detail. This study aimed to profile human Tg N-glycosylation sites and their glycan contents by using high-throughput glyco-analytical strategies, including glycopeptide and glycan levels. The sulfated complex and hybrid type N-glycan species were determined by the analysis of the human Tg samples with HPLC-HILIC-FLD-MS/MS. It was found that all fucosylated N-glycans carried fucose residue on their N-glycan core structure. The human Tg was digested with multiple enzymes by applying both in-gel and in-solution protocols to enhance site-specific glycosylation analysis. In total, 17 out of 20 N-glycosylation sites were characterized. It was noticed that 6 N-glycosylation sites contain only high-mannose type glycans, while other regions include complex and hybrid type glycans. In addition, sulfated glycoform structures were detected at the glycopeptide level in glycosylation sites containing complex and hybrid type glycans. It is expected that the results obtained from this study will contribute to functional studies to be conducted on human Tg protein. BIOLOGICAL SIGNIFICANCE: N-glycans of human thyroglobulin modulate thyroid hormone synthesis both in vivo and in vitro. Therefore, a comprehensive analysis of the N-glycosylation sites of human thyroglobulin is essential to improve our understanding of the function of its N-glycans. The present research significantly expanded the knowledge regarding N-glycosylation profiles of human thyroid thyroglobulin protein. For instance, as highlighted here, sulfated N-glycan structures were characterized using comprehensive glyco-analytical strategies. N-glycan patterns for the sites Asn110, Asn1869, and Asn2122 were described for the first time in this current work. In addition, N-glycan structures containing core-fucosylation and bisecting types were confirmed for all determined glycosylation sites.
MeSH term(s)	Glycopeptides/chemistry ; Glycosylation ; Humans ; Polysaccharides/chemistry ; Tandem Mass Spectrometry ; Thyroglobulin/chemistry ; Thyroglobulin/metabolism ; Thyroid Gland/metabolism
Chemical Substances	Glycopeptides ; Polysaccharides ; Thyroglobulin (9010-34-8)
Language	English
Publishing date	2022-08-19
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2400835-7
ISSN	1876-7737 ; 1874-3919
ISSN (online)	1876-7737
ISSN	1874-3919
DOI	10.1016/j.jprot.2022.104700
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Development and functionalization of electrospun fiber coated thin film microextraction devices for rapid mass spectrometric determination of biologically important polar molecules.

Öztürk, Merve / Salih, Bekir / Eroğlu, Ahmet E / Boyaci, Ezel

Journal of pharmaceutical and biomedical analysis

2024 Volume 243, Page(s) 116074

Abstract: Rapid diagnosis of diseases is one of the challenging areas in clinical research. From the analytical chemist's perspective, the main challenges are isolating the compounds from the bio-specimen and lengthy analysis times. In this regard, solid phase ... ...

Abstract	Rapid diagnosis of diseases is one of the challenging areas in clinical research. From the analytical chemist's perspective, the main challenges are isolating the compounds from the bio-specimen and lengthy analysis times. In this regard, solid phase microextraction offers a platform to address the abovementioned challenges. Moreover, its sharp tip-thin film geometry, known as coated blade spray (CBS), can enhance the extraction and act as an ionization source in direct mass spectrometric analysis. In this study, a new CBS device specifically designed for polar analytes was prepared and optimized to determine urinary metabolites. For this purpose, polyacrylonitrile (PAN) was selected as a base polymer as it can be electrospun to form a nanofibrous structure, and it can be modified with weak ion exchange moieties to interact with polar analytes. Following the electrospinning of PAN, hydrolysis was optimized, and conditions leading to sufficient extraction enhancement without dissolving the polymer were obtained when probes were treated with 5.0 M of NaOH for 2.5 h. Using the coated blades prepared as explained, the evaluation of various extraction conditions showed that 5 min is sufficient for equilibrium extraction. In addition, the solution's ionic strength and pH significantly affect the extraction. Optimum sorption was obtained at no salt added and pH 7.0 conditions. The CBS-MS optimization showed that 10.0 µL of ACN/MeOH/H
MeSH term(s)	Mass Spectrometry ; Solid Phase Microextraction/methods
Language	English
Publishing date	2024-02-27
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	604917-5
ISSN	1873-264X ; 0731-7085
ISSN (online)	1873-264X
ISSN	0731-7085
DOI	10.1016/j.jpba.2024.116074
Database	MEDical Literature Analysis and Retrieval System OnLINE

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ab Jg. 2022: Lesesaal (EG)

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Article ; Online: In vitro study on the competitive reactions between arsenite and selenite with glutathione.

Özkan, Canan Höçük / Atakay, Mehmet / Salih, Bekir / Ertaş, Gülay

Journal of mass spectrometry : JMS

2024 Volume 59, Issue 5, Page(s) e5020

Abstract: Exposure to arsenic can cause various biological effects by increasing the production of reactive oxygen species (ROS). Selenium acts as a beneficial element by regulating ROS and limiting heavy metal uptake and translocation. There are studies on the ... ...

Abstract	Exposure to arsenic can cause various biological effects by increasing the production of reactive oxygen species (ROS). Selenium acts as a beneficial element by regulating ROS and limiting heavy metal uptake and translocation. There are studies on the interactive effects of As and Se in plants, but the antagonistic and synergistic effects of these elements based on their binding to glutathione (GSH) molecules have not been studied yet. In this study, we aimed to investigate the antagonistic or synergistic effects of As and Se on the binding mechanism of Se and As with GSH at pH 3.0, 5.0, or 6.5. The interaction of As and Se in Se(SG)
MeSH term(s)	Glutathione/chemistry ; Glutathione/metabolism ; Arsenites/chemistry ; Selenious Acid/chemistry ; Tandem Mass Spectrometry/methods ; Spectrometry, Mass, Electrospray Ionization/methods ; Chromatography, Liquid/methods
Chemical Substances	Glutathione (GAN16C9B8O) ; Arsenites ; Selenious Acid (F6A27P4Q4R) ; arsenite (N5509X556J)
Language	English
Publishing date	2024-04-04
Publishing country	England
Document type	Journal Article
ZDB-ID	1221763-3
ISSN	1096-9888 ; 1076-5174
ISSN (online)	1096-9888
ISSN	1076-5174
DOI	10.1002/jms.5020
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Zs.A 4254: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MO 220: Show issues

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Article: Site-specific N-glycosylation analysis of human thyroid thyroglobulin by mass spectrometry-based Glyco-analytical strategies

Kayili, H. Mehmet / Salih, Bekir

Journal of proteomics. 2022 Sept. 15, v. 267

2022

Abstract	Human thyroglobulin (Tg), which has many glycosylation sites, is an essential protein produced by the human thyroid glands. Although human Tg N-glycans play critical roles in the cellular events of the Thyroid gland, the site-specific distribution of glycan structures has not been studied in detail. This study aimed to profile human Tg N-glycosylation sites and their glycan contents by using high-throughput glyco-analytical strategies, including glycopeptide and glycan levels. The sulfated complex and hybrid type N-glycan species were determined by the analysis of the human Tg samples with HPLC-HILIC-FLD-MS/MS. It was found that all fucosylated N-glycans carried fucose residue on their N-glycan core structure. The human Tg was digested with multiple enzymes by applying both in-gel and in-solution protocols to enhance site-specific glycosylation analysis. In total, 17 out of 20 N-glycosylation sites were characterized. It was noticed that 6 N-glycosylation sites contain only high-mannose type glycans, while other regions include complex and hybrid type glycans. In addition, sulfated glycoform structures were detected at the glycopeptide level in glycosylation sites containing complex and hybrid type glycans. It is expected that the results obtained from this study will contribute to functional studies to be conducted on human Tg protein. N-glycans of human thyroglobulin modulate thyroid hormone synthesis both in vivo and in vitro. Therefore, a comprehensive analysis of the N-glycosylation sites of human thyroglobulin is essential to improve our understanding of the function of its N-glycans. The present research significantly expanded the knowledge regarding N-glycosylation profiles of human thyroid thyroglobulin protein. For instance, as highlighted here, sulfated N-glycan structures were characterized using comprehensive glyco-analytical strategies. N-glycan patterns for the sites Asn110, Asn1869, and Asn2122 were described for the first time in this current work. In addition, N-glycan structures containing core-fucosylation and bisecting types were confirmed for all determined glycosylation sites.
Keywords	fucose ; glycopeptides ; glycosylation ; humans ; hybrids ; mass spectrometry ; polysaccharides ; proteomics ; thyroglobulin ; thyroid gland ; thyroid hormones
Language	English
Dates of publication	2022-0915
Publishing place	Elsevier B.V.
Document type	Article
ZDB-ID	2400835-7
ISSN	1876-7737 ; 1874-3919
ISSN (online)	1876-7737
ISSN	1874-3919
DOI	10.1016/j.jprot.2022.104700
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: N-glycan Profiling of Glycoproteins by Hydrophilic Interaction Liquid Chromatography with Fluorescence and Mass Spectrometric Detection.

Kayili, Haci Mehmet / Salih, Bekir

Journal of visualized experiments : JoVE

2021 , Issue 175

Abstract: Glycosylation is a vital modification found in proteins. N-glycan profiling of glycoproteins is required to detect novel biomarker candidates and determine glycan alterations in diseases. Most commercially available biopharmaceutical proteins are ... ...

Abstract	Glycosylation is a vital modification found in proteins. N-glycan profiling of glycoproteins is required to detect novel biomarker candidates and determine glycan alterations in diseases. Most commercially available biopharmaceutical proteins are glycoproteins. The efficacy of these drugs is affected by glycosylation patterns. Therefore, an in-depth characterization method for the N-glycans is necessary. Here, we present a comprehensive approach for qualitative and quantitative analysis of N-glycans using hydrophilic interaction liquid chromatography equipped with fluorescence detection and tandem mass spectrometry (HILIC-FLD-MS/MS). N-glycans were released from glycoproteins with a facile method and labeled by a procainamide fluorophore tag in the strategy. Subsequently, the procainamide labeled N-glycans were analyzed by a HILIC-FLD-MS/MS technique. In this approach, N-glycan structures were confirmed by the tandem mass spectrometric analysis, whereas fluorescence detection was used for the quantitative analysis. An application for data analysis of the detected N-glycan peaks is described in the study. This protocol can be applied to any glycoprotein extracted from various species.
MeSH term(s)	Chromatography, Liquid ; Glycoproteins ; Hydrophobic and Hydrophilic Interactions ; Polysaccharides ; Tandem Mass Spectrometry
Chemical Substances	Glycoproteins ; Polysaccharides
Language	English
Publishing date	2021-09-25
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Video-Audio Media
ZDB-ID	2259946-0
ISSN	1940-087X ; 1940-087X
ISSN (online)	1940-087X
ISSN	1940-087X
DOI	10.3791/62751
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: An integrated stage-tip-based glycomic and glycoproteomic approach for simple and rapid N-glycosylation profiling of glycoproteins.

Kayili, Hacı Mehmet / Ragoubi, Zidan M E / Salih, Bekir

Biomedical chromatography : BMC

2022 Volume 36, Issue 12, Page(s) e5503

Abstract: Glycosylation is a post-translational modification that plays an active role in many cellular events. It also regulates many functions of proteins. Monoclonal antibody-derived drugs are used to treat many diseases, and glycosylation affects the activity ... ...

Abstract	Glycosylation is a post-translational modification that plays an active role in many cellular events. It also regulates many functions of proteins. Monoclonal antibody-derived drugs are used to treat many diseases, and glycosylation affects the activity of such drugs developed. On the other hand, N-glycans may change in certain diseases. Therefore, rapid and efficient bioanalytical methods are needed for N-glycosylation profiling. The study aimed to develop an integrated stage-tip application for the simple and rapid N-glycosylation profiling of glycoproteins. A fast and inexpensive N-glycosylation profiling was achieved by integrating all glycoproteomic and glycomic sample preparation steps into a stage-tip. The glycomic approach of the integrated stage-tip reduces the N-glycan profiling time from 2 days to approximately 2.5 hours. It also allows the profiling of immunoglobulin G (IgG) N-glycopeptides directly from human plasma. In addition, N-glycosylation profiling can be done in the developed method without sorbents, C
MeSH term(s)	Humans ; Glycosylation ; Glycomics/methods ; Glycoproteins/metabolism ; Glycopeptides ; Polysaccharides
Chemical Substances	Glycoproteins ; Glycopeptides ; Polysaccharides
Language	English
Publishing date	2022-09-21
Publishing country	England
Document type	Journal Article
ZDB-ID	632848-9
ISSN	1099-0801 ; 0269-3879
ISSN (online)	1099-0801
ISSN	0269-3879
DOI	10.1002/bmc.5503
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Zs.A 2166: Show issues

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Article: Comparison of denaturing agent effects in enzymatic

Kayili, H Mehmet / Sakhta, Rokia / Salih, Bekir

Turkish journal of chemistry

2022 Volume 46, Issue 5, Page(s) 1524–1530

Abstract: Glycosylation is an essential posttranslational modification observed in the living proteome. Glycosylation profiles in glycoproteins can change in commonly observed diseases such as cancer. Identifying these changes is crucial in discovering new ... ...

Abstract	Glycosylation is an essential posttranslational modification observed in the living proteome. Glycosylation profiles in glycoproteins can change in commonly observed diseases such as cancer. Identifying these changes is crucial in discovering new biomarkers for the early diagnosis of cancer. One of the main steps of
Language	English
Publishing date	2022-05-20
Publishing country	Turkey
Document type	Journal Article
ZDB-ID	2046471-X
ISSN	1303-6130 ; 1300-0527
ISSN (online)	1303-6130
ISSN	1300-0527
DOI	10.55730/1300-0527.3457
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Synthesis and characterization of novel poly(α-methyl β-alanine-b-lactone)s through hydrogen-transfer and ring-opening polymerization

Çatiker, Efkan / Kirlak, Songül / Atakay, Mehmet / Salih, Bekir

Analele Universității "Ovidius" Constanța. 2022 Jan. 01, v. 33, no. 1

2022

Abstract: A series of novel poly(α-methyl β-alanine-b-lactone)s were prepared by a combination of hydrogen-transfer polymerization (HTP) of methacrylamide (MAm) and anionic ring-opening polymerization (AROP) of β-propiolactone (BPL), β-butyrolactone (BBL), and δ- ... ...

Abstract	A series of novel poly(α-methyl β-alanine-b-lactone)s were prepared by a combination of hydrogen-transfer polymerization (HTP) of methacrylamide (MAm) and anionic ring-opening polymerization (AROP) of β-propiolactone (BPL), β-butyrolactone (BBL), and δ-valerolactone (DVL). For this purpose, poly(α-methyl β-alanine) (PmBA) having a living anionic end-group for a further extension was obtained via HTP of MAm. The anionic end-group on PmBA chains were used as initiation sites for AROP of BPL, BBL, and DVL. Fourier Transform Infrared Spectroscopy (FTIR) and Proton Nuclear Magnetic Resonance Spectroscopy (¹H-NMR) confirmed the existence of both ester and α-methyl β-alanine (mBA) units in the final products. MALDI-MS analysis revealed that the poly(α-methyl β-alanine-b-lactone)s with average molar masses of several thousand g·mol⁻¹ were obtained. DSC and TGA thermograms of each copolymer showed that the copolymers comprised the mBA and the corresponding ester units.
Keywords	Fourier transform infrared spectroscopy ; composite polymers ; nuclear magnetic resonance spectroscopy ; polymerization
Language	English
Dates of publication	2022-0101
Size	p. 78-83.
Publishing place	Sciendo
Document type	Article
ISSN	2286-038X
DOI	10.2478/auoc-2022-0011
Database	NAL-Catalogue (AGRICOLA)

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