prikaz prve stranice dokumenta Istraživanje RET i vezajućih partnera efrin-A2 i efrin-A5b
Access restricted to students and staff of home institution
master's thesis
Istraživanje RET i vezajućih partnera efrin-A2 i efrin-A5b
Zagreb: University of Zagreb, Faculty of Food Technology and Biotechnology, 2015. urn:nbn:hr:159:511555
Pavić, Ana
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

Pavić, A. (2015). Istraživanje RET i vezajućih partnera efrin-A2 i efrin-A5b (Master's thesis). Zagreb: University of Zagreb, Faculty of Food Technology and Biotechnology. Retrieved from https://urn.nsk.hr/urn:nbn:hr:159:511555

Pavić, Ana. "Istraživanje RET i vezajućih partnera efrin-A2 i efrin-A5b." Master's thesis, University of Zagreb, Faculty of Food Technology and Biotechnology, 2015. https://urn.nsk.hr/urn:nbn:hr:159:511555

Pavić, Ana. "Istraživanje RET i vezajućih partnera efrin-A2 i efrin-A5b." Master's thesis, University of Zagreb, Faculty of Food Technology and Biotechnology, 2015. https://urn.nsk.hr/urn:nbn:hr:159:511555

Pavić, A. (2015). 'Istraživanje RET i vezajućih partnera efrin-A2 i efrin-A5b', Master's thesis, University of Zagreb, Faculty of Food Technology and Biotechnology, accessed 30 November 2024, https://urn.nsk.hr/urn:nbn:hr:159:511555

Pavić A. Istraživanje RET i vezajućih partnera efrin-A2 i efrin-A5b [Master's thesis]. Zagreb: University of Zagreb, Faculty of Food Technology and Biotechnology; 2015 [cited 2024 November 30] Available at: https://urn.nsk.hr/urn:nbn:hr:159:511555

A. Pavić, "Istraživanje RET i vezajućih partnera efrin-A2 i efrin-A5b", Master's thesis, University of Zagreb, Faculty of Food Technology and Biotechnology, Zagreb, 2015. Available at: https://urn.nsk.hr/urn:nbn:hr:159:511555

Metadata
TitleIstraživanje RET i vezajućih partnera efrin-A2 i efrin-A5b
Title (english)Studies of RET and its binding partners ephrin-A2 and ephrin-A5b
AuthorAna Pavić
MentorVladimir Mrša (mentor)
GranterUniversity of Zagreb
Faculty of Food Technology and Biotechnology
(Department of Chemistry and Biochemistry)
(Laboratory for Biochemistry)
Zagreb
Defense date and country2015-12-16, Croatia
Scientific / art field,
discipline and subdiscipline		BIOTECHNICAL SCIENCES
Biotechnology
Abstract
Eph receptor tirozin kinaze i njegovi ligandi, efrini imaju važnu ulogu u različitim biološkim funkcijama. Trenutna istraživanja usmjerena su na ulogu efrin-A reverznog signala u razvoju neurona, budući da se pretpostavlja da je posredovan RET-transmembranskim tirozin kinaza ko-receptorom. Cilj istraživanja bio je klonirati, eksprimirati i pročistiti ekstracelularne domene efrin-A2 i efrin-A5b proteina iz zebrice (Danio rerio). Kloniranje korištenjem restrikcijskih enzima NotI i XbaI je provedeno u pk503.9-FLAG-8xHis-Thr vektoru izvedenom iz pFastBac-1. Bakulovirus-sustav ekspresije pokazao se uspješnijim za efrin-A5b nego za efrin-A2. Proteini su pročišćeni iz medija afinitetnom kromatografijom i gel filtracijom. Budući da je dobivena veća koncentracija čistog efrin-A5b, korišten je za studije vezivanja s RET. Rezultati “pull-down” testa nisu jasni i daljnja istraživanja su nužna kako bi se potvrdilo specifično vezivanje RET.
Abstract (english)
Eph receptor tyrosine kinases and their ligands, the ephrins perform an important function in different biological functions. Recent work focused on the role of ephrin-A reverse signaling in neuronal development as it has been hypothesized to be mediated by RET-a transmembrane tyrosine kinase co-receptor. The goal of this project was to clone, express and purify the extracelullar domains of ephrin-A2 and ephrin-A5b proteins from zebrafish (Danio rerio). Cloning was done into the expression vector pFastBac-1 derivative pk503.9-FLAG-8xHis-Thr using restriction enzymes NotI and XbaI. Baculovirus-expression system showed to be more successful for ephrin-A5b than for ephrin-A2. Proteins were purified from the media by affinity chromatography and gel-filtration. Since the higher yield of pure ephrin-A5b was obtained, it was used for binding studies with RET. Results of „pull-down“ assay are not conclusive and further analysis are required in order to confirm specific binding of RET.
Keywords
Keywords (english)
Languageenglish
URN:NBNurn:nbn:hr:159:511555
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 on2017-04-27 09:22:36