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master's thesis
Biokemijska i biofizička karakterizacija domene G ljudskog gvanilat vezujućeg protein 3 (hGBP3)
Zagreb: University of Zagreb, Faculty of Science, 2012. urn:nbn:hr:217:962104
Kovačević, Marija
University of Zagreb
Faculty of Science
Department of Biology

Institutional repository: Repository of the Faculty of Science

Cite this document

Kovačević, M. (2012). Biokemijska i biofizička karakterizacija domene G ljudskog gvanilat vezujućeg protein 3 (hGBP3) (Master's thesis). Zagreb: University of Zagreb, Faculty of Science. Retrieved from https://urn.nsk.hr/urn:nbn:hr:217:962104

Kovačević, Marija. "Biokemijska i biofizička karakterizacija domene G ljudskog gvanilat vezujućeg protein 3 (hGBP3)." Master's thesis, University of Zagreb, Faculty of Science, 2012. https://urn.nsk.hr/urn:nbn:hr:217:962104

Kovačević, Marija. "Biokemijska i biofizička karakterizacija domene G ljudskog gvanilat vezujućeg protein 3 (hGBP3)." Master's thesis, University of Zagreb, Faculty of Science, 2012. https://urn.nsk.hr/urn:nbn:hr:217:962104

Kovačević, M. (2012). 'Biokemijska i biofizička karakterizacija domene G ljudskog gvanilat vezujućeg protein 3 (hGBP3)', Master's thesis, University of Zagreb, Faculty of Science, accessed 23 December 2024, https://urn.nsk.hr/urn:nbn:hr:217:962104

Kovačević M. Biokemijska i biofizička karakterizacija domene G ljudskog gvanilat vezujućeg protein 3 (hGBP3) [Master's thesis]. Zagreb: University of Zagreb, Faculty of Science; 2012 [cited 2024 December 23] Available at: https://urn.nsk.hr/urn:nbn:hr:217:962104

M. Kovačević, "Biokemijska i biofizička karakterizacija domene G ljudskog gvanilat vezujućeg protein 3 (hGBP3)", Master's thesis, University of Zagreb, Faculty of Science, Zagreb, 2012. Available at: https://urn.nsk.hr/urn:nbn:hr:217:962104

Metadata
TitleBiokemijska i biofizička karakterizacija domene G ljudskog gvanilat vezujućeg protein 3 (hGBP3)
Title (english)Biochemical and biophysical characterization of G domain of human guanylate binding protein 3 (hGBP3)
AuthorMarija Kovačević
MentorNada Oršolić (mentor)
Committee memberNada Oršolić (predsjednik povjerenstva)
Committee memberMirjana Kalafatić (član povjerenstva)
Committee memberMirjana Pavlica (član povjerenstva)
Committee memberSven Jelaska (član povjerenstva)
GranterUniversity of Zagreb
Faculty of Science
(Department of Biology)
Zagreb
Defense date and country2012-04-17, Croatia
Scientific / art field,
discipline and subdiscipline		NATURAL SCIENCES
Biology
Abstract
Ljudski gvanilat vezujući protein 3 pripada grupi interferonom induciranih GTPaza i uključen je u urođeni imunosni odgovor. Jedan od ključnih procesa u obavljanju njegove funkcije je hidroliza, koja se odvija na velikoj G (LG) domeni. Ciljevi ovog rada su bili purifikacija i determinacija osnovnih biokemijskih i biofizičkih karakteristika. Analiza vezenja za nukleotide i kinetika su pokazala da je raspon vezanja nukleotida za protein mikromolarni, iako manji u slučaju GTP analoga, a viši kod m-GMP-a i m- GDP-a. Hidrolitička aktivnost je bila manja u usporedbi s referentnim hGBP1 LG (44. 1 min⁻¹), 22.8 min⁻¹ i konstanta disocijacije je bila 1.3 μM. Analitička gel filtracija je pokazala da je protein monomeran, te da ne pokazuje oligomerizaciju ovisnu o nukleotidima, no pretpostavlja se da je ovo bio slučaj zbog visoke koncentracije soli. hGBP3 LG pokazuje karakteristike tipične za GBP porodicu, iako se treba napraviti još istraživanja da bi se dobila kompletna biokemijska i biofizička analiza.
Abstract (english)
Human guanylate binding protein 3 is one of the members of interferon inducible GTPases and is a protein involved in innate immune response. One of the key processes in preforming its function is hydrolysis, which takes place on large GTPase (LG) domain. Aims of this work were to purify the protein and to determine basic biochemical and biophysical features. Analysis of nucleotide binding and its kinetics showed that the range of nucleotide- protein binding is micromolar, although lower in the case of GTP analogues, and higher in m-GMP and m-GDP. Hydrolytic activity was lower in comparison to refered hGBP1 LG (44. 1 min⁻¹), 22.8 min⁻¹, and dissociation constant was 1.3 μM. Analytical gel filtration showed that the protein is monomeric, without showing nucleotide dependent oligomerization, but it is assumed that this was due to high salt concentration. It shows characteristics typical for GBP family, although more researches need to be done to complete the whole biochemical and biophysical analysis.
Keywords
Keywords (english)
Languagecroatian
URN:NBNurn:nbn:hr:217:962104
Study programmeTitle: Experimental Biology
Study programme type: university
Study level: graduate
Academic / professional title: magistar/magistra eksperimentalne biologije (magistar/magistra eksperimentalne biologije)
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 09:08:07