Biochemical and biophysical characterization of G domain of human guanylate binding protein 3 (hGBP3)

Kovačević, Marija (2012) Biochemical and biophysical characterization of G domain of human guanylate binding protein 3 (hGBP3). Diploma thesis, Faculty of Science > Department of Biology.

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Abstract

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.

Item Type: Thesis (Diploma thesis)
Keywords: hGBP3, G domain, hydrolysis, nucleotide binding, nucleotide dependent oligomerization
Supervisor: Hermann, Christian
Co-supervisor: Oršolić, Nada
Date: 2012
Number of Pages: 41
Subjects: NATURAL SCIENCES > Biology
Divisions: Faculty of Science > Department of Biology
Depositing User: Grozdana Sirotic
Date Deposited: 03 Jun 2014 12:27
Last Modified: 19 Sep 2014 11:03
URI: http://digre.pmf.unizg.hr/id/eprint/2167

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