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master's thesis
Strukturna analiza N-glikanskog profila ukupnih proteina plazme miša soja DBA/2 HILIC-UPLC-FLR-MS/MS metodom
Zagreb: University of Zagreb, Faculty of Pharmacy and Biochemistry, 2018. urn:nbn:hr:163:952762
Korman, Josipa
University of Zagreb
Faculty of Pharmacy and Biochemistry
Department of biochemistry and molecular biology

Institutional repository: Repository of Faculty of Pharmacy and Biochemistry University of Zagreb

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Korman, J. (2018). Strukturna analiza N-glikanskog profila ukupnih proteina plazme miša soja DBA/2 HILIC-UPLC-FLR-MS/MS metodom (Master's thesis). Zagreb: University of Zagreb, Faculty of Pharmacy and Biochemistry. Retrieved from https://urn.nsk.hr/urn:nbn:hr:163:952762

Korman, Josipa. "Strukturna analiza N-glikanskog profila ukupnih proteina plazme miša soja DBA/2 HILIC-UPLC-FLR-MS/MS metodom." Master's thesis, University of Zagreb, Faculty of Pharmacy and Biochemistry, 2018. https://urn.nsk.hr/urn:nbn:hr:163:952762

Korman, Josipa. "Strukturna analiza N-glikanskog profila ukupnih proteina plazme miša soja DBA/2 HILIC-UPLC-FLR-MS/MS metodom." Master's thesis, University of Zagreb, Faculty of Pharmacy and Biochemistry, 2018. https://urn.nsk.hr/urn:nbn:hr:163:952762

Korman, J. (2018). 'Strukturna analiza N-glikanskog profila ukupnih proteina plazme miša soja DBA/2 HILIC-UPLC-FLR-MS/MS metodom', Master's thesis, University of Zagreb, Faculty of Pharmacy and Biochemistry, accessed 23 December 2024, https://urn.nsk.hr/urn:nbn:hr:163:952762

Korman J. Strukturna analiza N-glikanskog profila ukupnih proteina plazme miša soja DBA/2 HILIC-UPLC-FLR-MS/MS metodom [Master's thesis]. Zagreb: University of Zagreb, Faculty of Pharmacy and Biochemistry; 2018 [cited 2024 December 23] Available at: https://urn.nsk.hr/urn:nbn:hr:163:952762

J. Korman, "Strukturna analiza N-glikanskog profila ukupnih proteina plazme miša soja DBA/2 HILIC-UPLC-FLR-MS/MS metodom", Master's thesis, University of Zagreb, Faculty of Pharmacy and Biochemistry, Zagreb, 2018. Available at: https://urn.nsk.hr/urn:nbn:hr:163:952762

Metadata
TitleStrukturna analiza N-glikanskog profila ukupnih proteina plazme miša soja DBA/2 HILIC-UPLC-FLR-MS/MS metodom
Title (english)Structural analysis of murine plasma N-glycome from DBA/2 strain with HILIC-UPLC-FLR-MS/MS method
AuthorJosipa Korman
MentorOlga Gornik (mentor)
Committee memberToma Keser (predsjednik povjerenstva)
Committee memberAna Mornar Turk (član povjerenstva)
Committee memberTamara Pavić (član povjerenstva)
GranterUniversity of Zagreb
Faculty of Pharmacy and Biochemistry
(Department of biochemistry and molecular biology)
Zagreb
Defense date and country2018-06-28, Croatia
Scientific / art field,
discipline and subdiscipline		BIOMEDICINE AND HEALTHCARE
Pharmacy
Pharmacy
Abstract
Glikozilacija proteina je složena kotranslacijska i postranslacijska modifikacija posredovana enzimima u kojoj dolazi do kovalentnog vezanja šećernih struktura na proteine. Glikanski dio utječe na svojstva i funkciju glikoproteina. Istraživanjima se sve više utvrđuje povezanost glikana s različitim patofiziološkim stanjima te zbog toga oni postaju predmetom sve brojnijih istraživanja. Budući da se miševi vrlo često koriste kao eksperimentalni model istraživanja humanih bolesti, važno je istražiti razlike u glikozilaciji između humanih i mišjih proteina, te ih uzeti u obzir prilikom odabira životinjskog modela. U ovom radu su analizirani N-glikani plazme miša soja DBA/2 HILIC-UPLC-FLR-MS/MS metodom u pozitivnom ionskom modu. Kao rezultat, prikazan je FLR kromatogram sa asigniranim odgovarajućim glikanskim strukturama na temelju MS/MS spektra i programa GlycoWorkbench 2. Pronađeni su oligomanozni, hibridni i kompleksni glikani, sveukupno 31 različit N-vezani glikan. Analizirani glikani koji sadrže sijalinsku kiselinu, imaju N-glikolilneuraminsku kiselinu, što je važna razlika u odnosu na humane glikane koji sadrže isključivo N-acetilneuraminsku kiselinu.
Abstract (english)
Protein glycosylation is a complex cotranslational and posttranslational enzyme-mediated modification, in which the sugar structures covalently bind to proteins. The glycan part affects the properties and function of glycoproteins. Glycans are being associated with different pathophysiological conditions and therefore become the subject of ever increasing research. Since mice are very often used as an experimental model of human disease research, it is important to investigate the differences in glycosylation between human and mouse proteins and to consider them when deciding between animal models. This Master thesis analyses the plasma N-glycosilation of mice from DBA strain using positive ion mode HILIC-UPLC-FLR-MS/MS method. As a result, the FLR chromatogram is presented with assigned glycan structures obtained from MS/MS spectrum and GlycoWorkbench 2.1 program. Oligomannose, hybrid and complex glycans were found, altogether 31 different N-linked glycan. The analyzed glycans which contain sialic acid have N-glycolylneuraminic acid, which is an important difference compared to human glycans which contain exclusively N-acetylneuramic acid.
Keywords
Keywords (english)
Languagecroatian
URN:NBNurn:nbn:hr:163:952762
Study programmeTitle: Pharmacy
Study programme type: university
Study level: integrated undergraduate and graduate
Academic / professional title: magistar/magistra farmacije (magistar/magistra farmacije)
Type of resourceText
File originBorn digital
Access conditionsOpen access
Terms of useLicence In copyright icon
Created on2019-01-16 08:39:18