| Records |
| Author |
Vagin, M.Y.; Trashin, S.A.; Beloglazkina, E.K.; Majouga, A.G. |
| Title |
Direct reagentless detection of the affinity binding of recombinant His-tagged firefly luciferase with a nickel-modified gold electrode |
Type |
A1 Journal article |
Year  |
2015 |
Publication |
Mendeleev communications |
Abbreviated Journal |
|
| Volume |
25 |
Issue |
4 |
Pages |
290-292 |
| Keywords |
A1 Journal article; AXES (Antwerp X-ray Analysis, Electrochemistry and Speciation) |
| Abstract |
The direct reagentless electrochemical detection of recombinant firefly luciferase binding with a gold electrode modified with nickel complex of 1,16-di[4-(2,6-dihydroxycarbonyl)pyridyl]-1,16-dioxa-8,9-dithiahexadecane has been carried out. |
| Address |
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| Corporate Author |
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Thesis |
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| Publisher |
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Place of Publication |
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Editor |
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| Language |
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Wos |
000360416600021 |
Publication Date |
2015-08-07 |
| Series Editor |
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Series Title |
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Abbreviated Series Title |
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| Series Volume |
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Series Issue |
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Edition |
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| ISSN |
0959-9436 |
ISBN |
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Additional Links |
UA library record; WoS full record; WoS citing articles |
| Impact Factor |
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Times cited |
|
Open Access |
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| Notes |
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Approved |
no |
| Call Number |
UA @ admin @ c:irua:127814 |
Serial |
7811 |
| Permanent link to this record |
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| Author |
Borhani, A.H.; Berghmans, H.; Trashin, S.; De Wael, K.; Fago, A.; Moens, L.; Habibi-Rezaei, M.; Dewilde, S. |
| Title |
Kinetic properties and heme pocket structure of two domains of the polymeric hemoglobin of Artemia in comparison with the native molecule |
Type |
A1 Journal article |
| Year |
2015 |
Publication |
Biochimica et biophysica acta : proteins and proteomics |
Abbreviated Journal |
Bba-Proteins Proteom |
| Volume |
1854 |
Issue |
10a |
Pages |
1307-1316 |
| Keywords |
A1 Journal article; AXES (Antwerp X-ray Analysis, Electrochemistry and Speciation) |
| Abstract |
In this project, we studied some physicochemical properties of two different globin domains of the polymeric hemoglobin of the brine shrimp Artemia salina and compared them with those of the native molecule. Two domains (AsHbC1D1 and AsHbC1D5) were cloned and expressed in BL21(DE3)pLysS strain of Escherichiacoli. The recombinant proteins as well as the native hemoglobin (AfHb) were purified from bacteria and frozen Artemia, respectively by standard chromatographic methods and assessed by SDS-PAGE. The heme environment of these proteins was studied by optical spectroscopy and ligand-binding kinetics (e.g. CO association and O2 binding affinity) were measured for the two recombinant proteins and the native hemoglobin. This indicates that the CO association rate for AsHbC1D1 is higher than that of AsHbC1D5 and AfHb, while the calculated P50 value for AsHbC1D1 is lower than that of AsHbC1D5 and AfHb. The geminate and bimolecular rebinding parameters indicate a significant difference between both domains. Moreover, EPR results showed that the heme pocket in AfHb is in a more closed conformation than the heme pocket in myoglobin. Finally, the reduction potential of − 0.13 V versus the standard hydrogen electrode was determined for AfHb by direct electrochemical measurements. It is about 0.06 V higher than the potential of the single domain AsHbC1D5. This work shows that each domain in the hemoglobin of Artemia has different characteristics of ligand binding. |
| Address |
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| Corporate Author |
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Thesis |
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| Publisher |
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Place of Publication |
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Editor |
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| Language |
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Wos |
000362307500008 |
Publication Date |
2015-05-22 |
| Series Editor |
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Series Title |
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Abbreviated Series Title |
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| Series Volume |
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Series Issue |
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Edition |
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| ISSN |
1570-9639 |
ISBN |
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Additional Links |
UA library record; WoS full record |
| Impact Factor |
2.773 |
Times cited |
|
Open Access |
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| Notes |
; This work was supported by the general grant for visiting scholar of the Ministry of Science, Research and Technology of I. R. Iran and by the University of Antwerp. ; |
Approved |
Most recent IF: 2.773; 2015 IF: 2.747 |
| Call Number |
UA @ admin @ c:irua:125909 |
Serial |
5683 |
| Permanent link to this record |
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| Author |
Trashin, S.; De Jong, M.; Breugelmans, T.; Pilehvar, S.; De Wael, K. |
| Title |
Label-free impedance aptasensor for major peanut allergen Ara h 1 |
Type |
A1 Journal article |
| Year |
2015 |
Publication |
Electroanalysis |
Abbreviated Journal |
|
| Volume |
27 |
Issue |
1 |
Pages |
32-37 |
| Keywords |
A1 Journal article; Engineering sciences. Technology; AXES (Antwerp X-ray Analysis, Electrochemistry and Speciation); Applied Electrochemistry & Catalysis (ELCAT) |
| Abstract |
The peanut allergen Ara h 1 belonging to the vicilin family of seed storage proteins is known to be a suitable marker for peanut detection in foods. In the present work, we suggest an electrochemical detection of Ara h 1 using a recently selected 80-base DNA aptamer. The detection strategy relies on insulation effect of a bulky protein captured by an immobilized aptamer. The electrodes were modified by the aptamer and characterized using electrochemical impedance spectroscopy (EIS). The aptamer surface density and analytical parameters of the calibration curves for Ara h 1 were compared with the system prepared with thrombin binding aptamer (TBA) and operated in the same conditions. |
| Address |
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| Corporate Author |
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Thesis |
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| Publisher |
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Place of Publication |
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Editor |
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| Language |
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Wos |
000347838300004 |
Publication Date |
2014-10-13 |
| Series Editor |
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Series Title |
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Abbreviated Series Title |
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| Series Volume |
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Series Issue |
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Edition |
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| ISSN |
|
ISBN |
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Additional Links |
UA library record; WoS full record; WoS citing articles |
| Impact Factor |
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Times cited |
10 |
Open Access |
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| Notes |
; ST greatly appreciates the Research Council University of Antwerp (IWS BOF UA) for funding the post-doctoral fellowship. ; |
Approved |
Most recent IF: NA |
| Call Number |
UA @ admin @ c:irua:119442 |
Serial |
5686 |
| Permanent link to this record |
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| Author |
Anaf, W.; Trashin, S.; Schalm, O.; van Dorp, D.; Janssens, K.; De Wael, K. |
| Title |
Electrochemical photodegradation study of semiconductor pigments : influence of environmental parameters |
Type |
A1 Journal article |
| Year |
2014 |
Publication |
Analytical chemistry |
Abbreviated Journal |
Anal Chem |
| Volume |
86 |
Issue |
19 |
Pages |
9742-9748 |
| Keywords |
A1 Journal article; AXES (Antwerp X-ray Analysis, Electrochemistry and Speciation); Antwerp Cultural Heritage Sciences (ARCHES) |
| Abstract |
Chemical transformations in paintings often induce discolorations, disturbing the appearance of the image. For an appropriate conservation of such valuable and irreplaceable heritage objects, it is important to have a good know-how on the degradation processes of the (historical) materials: which pigments have been discolored, what are the responsible processes, and which (environmental) conditions have the highest impact on the pigment degradation and should be mitigated. Pigment degradation is already widely studied, either by analyzing historical samples or by accelerated weathering experiments on dummies. However, in historic samples several processes may have taken place, increasing the complexity of the current state, while aging experiments are time-consuming due to the often extended aging period. An alternative method is proposed for a fast monitoring of degradation processes of semiconductor pigments, using an electrochemical setup mimicking the real environment and allowing the identification of harmful environmental parameters for each pigment. Examples are given for the pigments cadmium yellow (CdS) and vermilion (α-HgS). |
| Address |
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| Corporate Author |
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Thesis |
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| Publisher |
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Place of Publication |
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Editor |
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| Language |
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Wos |
000343017100058 |
Publication Date |
2014-08-27 |
| Series Editor |
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Series Title |
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Abbreviated Series Title |
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| Series Volume |
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Series Issue |
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Edition |
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| ISSN |
0003-2700; 5206-882x |
ISBN |
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Additional Links |
UA library record; WoS full record; WoS citing articles |
| Impact Factor |
6.32 |
Times cited |
18 |
Open Access |
|
| Notes |
; ; |
Approved |
Most recent IF: 6.32; 2014 IF: 5.636 |
| Call Number |
UA @ admin @ c:irua:118834 |
Serial |
5593 |
| Permanent link to this record |
