prikaz prve stranice dokumenta Htm2- Specifičan enzim iz kvasca Saccharomyces cerevisiae
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master's thesis
Htm2- Specifičan enzim iz kvasca Saccharomyces cerevisiae
Zagreb: University of Zagreb, Faculty of Food Technology and Biotechnology, 2014. urn:nbn:hr:159:999380
Patron, Iva
University of Zagreb
Faculty of Food Technology and Biotechnology
Department of Chemistry and Biochemistry
Laboratory for Biochemistry

Institutional repository: Repository of the Faculty of Food Technology and Biotechnology

Cite this document

Patron, I. (2014). Htm2- Specifičan enzim iz kvasca Saccharomyces cerevisiae (Master's thesis). Zagreb: University of Zagreb, Faculty of Food Technology and Biotechnology. Retrieved from https://urn.nsk.hr/urn:nbn:hr:159:999380

Patron, Iva. "Htm2- Specifičan enzim iz kvasca Saccharomyces cerevisiae." Master's thesis, University of Zagreb, Faculty of Food Technology and Biotechnology, 2014. https://urn.nsk.hr/urn:nbn:hr:159:999380

Patron, Iva. "Htm2- Specifičan enzim iz kvasca Saccharomyces cerevisiae." Master's thesis, University of Zagreb, Faculty of Food Technology and Biotechnology, 2014. https://urn.nsk.hr/urn:nbn:hr:159:999380

Patron, I. (2014). 'Htm2- Specifičan enzim iz kvasca Saccharomyces cerevisiae', Master's thesis, University of Zagreb, Faculty of Food Technology and Biotechnology, accessed 27 December 2024, https://urn.nsk.hr/urn:nbn:hr:159:999380

Patron I. Htm2- Specifičan enzim iz kvasca Saccharomyces cerevisiae [Master's thesis]. Zagreb: University of Zagreb, Faculty of Food Technology and Biotechnology; 2014 [cited 2024 December 27] Available at: https://urn.nsk.hr/urn:nbn:hr:159:999380

I. Patron, "Htm2- Specifičan enzim iz kvasca Saccharomyces cerevisiae", Master's thesis, University of Zagreb, Faculty of Food Technology and Biotechnology, Zagreb, 2014. Available at: https://urn.nsk.hr/urn:nbn:hr:159:999380

Metadata
TitleHtm2- Specifičan enzim iz kvasca Saccharomyces cerevisiae
Title (english)Htm2-A specific enzyme from yeast Saccharomyces cerevisiae
AuthorIva Patron
MentorVladimir Mrša (mentor)
GranterUniversity of Zagreb
Faculty of Food Technology and Biotechnology
(Department of Chemistry and Biochemistry)
(Laboratory for Biochemistry)
Zagreb
Defense date and country2014-09-23, Croatia
Scientific / art field,
discipline and subdiscipline		BIOTECHNICAL SCIENCES
Biotechnology
Abstract
U eukariotskim stanicama, membranski proteini i topljivi proteini sekretornog puta nakon sinteze ulaze u endoplazmatski retikulum (ER) u nesmotanom obliku. Direktno nakon ulaska u ER, većina proteina je glikolizirana odrađenim ugljikohidratima na određenom mjestu glikozilacije nakon čega proteini započinju smatanje. Protein koji se ne može pravilno smotati, bit će obilježen i degradiran u procesu nazvanom razgradnja proteina u endoplazmatskom retikulumu. Istraživanja su pokazala da se tijekom procesa N-glikozilacije proteina, značajna količina slobodnih oligosaharida sintetizira u ER-u. Slobodni oligosaharidi se također sintetiziraju u citosolu enzimskim procesom deglikozilacije krivo smotanih glikoproteina. Pogreške pri razgradnji proteina u ER-u, bilo gubitkom funkcije ili preranom degradacijom proteina, uzrokuju brojne teške bolesti. Upravo zbog toga, otkrivanje novih komponenata sustava za razgradnju proteina u ER-u kako bi ga bolje razumijeli, od izrazite je važnosti. U ovom radu, nova potencijalna kvaščeva manozidaza, Htm2 poznata i kao Mnl2, je identificirana i istraživana, a istraživanja su pokazala da se nalazi u Golgijevom aparatu.
Abstract (english)
In eukaryotes, membrane and soluble proteins of the secretory pathway enter the endoplasmic reticulum (ER) after synthesis in an unfolded state. Directly after entry, most proteins are modified with glycans at suitable glycosylation sites and start to fold. A protein that cannot fold properly will be degraded in a process called ER associated degradation (ERAD). It has been shown that during the N-glycosylation of proteins, significant amounts of free oligosaccharides are generated in the lumen of the ER. Free OSs are also formed in the cytosol by enzymatic deglycosylation of misfolded glycoproteins. Failures in ERAD, either by loss of function or by premature degradation of proteins, are a cause of severe disease. Therefore, the search for novel ERAD components to gain better insight in this process is of high importance. In this work a novel putative yeast mannosidase, named Htm2 also known as Mnl2, located in Golgi was explored and identified.
Keywords
Keywords (english)
Languagecroatian
URN:NBNurn:nbn:hr:159:999380
Study programmeTitle: Molecular Biotechnology
Study programme type: university
Study level: graduate
Academic / professional title: magistar/magistra inženjer/inženjerka molekularne biotehnologije (magistar/magistra inženjer/inženjerka molekularne biotehnologije)
Type of resourceText
File originBorn digital
Access conditionsAccess restricted to students and staff of home institution
Terms of useLicence In copyright icon
Created on2017-05-02 10:42:26