Probing the structure of macromolecules using microsecond time-resolved fluorescence of europium chelates

1998 ◽  
Author(s):  
Ewa Heyduk ◽  
Tomasz Heyduk
Keyword(s):  
Time Resolved Fluorescence ◽  
Time Resolved ◽  
Europium Chelates

scholarly journals The use of peroxidase-mediated deposition of biotin-tyramide in combination with time-resolved fluorescence imaging of europium chelate label in immunohistochemistry and in situ hybridization.

1996 ◽  
Vol 44 (10) ◽  
pp. 1091-1099 ◽  
Author(s):  
R R de Haas ◽  
N P Verwoerd ◽  
M P van der Corput ◽  
R P van Gijlswijk ◽  
H Siitari ◽  
...  
Keyword(s):  
In Situ Hybridization ◽  
Elongation Factor ◽  
Delayed Fluorescence ◽  
Time Resolved Fluorescence ◽  
Time Resolved ◽  
Amplification System ◽  
Luciferase Mrna ◽  
Europium Chelate ◽  
Europium Chelates

The application of europium chelates as delayed fluorescent labels in FISH and immunocytochemistry is hampered by their relatively low quantum yield. To increase the intensity of the delayed fluorescence, we have used a recently introduced peroxidase-mediated amplification system. This system results in a large accumulation of biotin-tyramide, which is detected using streptavidin-europium chelate as label. Optimal staining conditions were evaluated for the immunocytochemical detection of vimentin in cryosections of rat liver, for DNA in situ hybridization (alphoid type probes and 40-KB cosmid probes), and for RNA in situ hybridization (detection of 28S ribosomal RNA, human elongation factor mRNA, and luciferase mRNA). Using a time-resolved fluorescence microscope, intense europium fluorescence was obtained in all these applications when the tyramide amplification system was applied. The signals were strong enough to be observed by eye using the microscope in the time-delayed mode. The routine application of this technique for localization and quantization of antigens or nucleic acid sequences in tissue exhibiting strong autofluorescence is discussed.

scholarly journals The influence of sugar–protein complexes on the thermostability of C-reactive protein (CRP)

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Andreea Lorena Mateescu ◽  
Nicolae-Bogdan Mincu ◽  
Silvana Vasilca ◽  
Roxana Apetrei ◽  
Diana Stan ◽  
...  
Keyword(s):  
Diagnostic Tests ◽  
Protein Complexes ◽  
C Reactive Protein ◽  
Time Resolved Fluorescence ◽  
Time Resolved ◽  
Reactive Protein ◽  
In Vitro Diagnostic ◽  
The Stability ◽  
Positive Controls

AbstractThe purpose of the present study was to evaluate de influence of protein–sugar complexation on the stability and functionality of C-reactive protein, after exposure to constant high temperatures, in order to develop highly stable positive controls for in-vitro diagnostic tests. C-reactive protein is a plasmatic protein used as a biomarker for the diagnosis of a series of health problems such as ulcerative colitis, cardiovascular diseases, metabolic syndrome, due to its essential role in the evolution of chronic inflammation. The sugar–protein interaction was investigated using steady state and time resolved fluorescence. The results revealed that there are more than two classes of tryptophan, with different degree of accessibility for the quencher molecule. Our study also revealed that sugar–protein complexes have superior thermostability, especially after gamma irradiation at 2 kGy, the protein being stable and functional even after 22 days exposure to 40 °C.

scholarly journals Architecture of Polyglutamine-containing Fibrils from Time-resolved Fluorescence Decay

2014 ◽  
Vol 289 (39) ◽  
pp. 26817-26828 ◽  
Author(s):  
Christoph Röthlein ◽  
Markus S. Miettinen ◽  
Tejas Borwankar ◽  
Jörg Bürger ◽  
Thorsten Mielke ◽  
...  
Keyword(s):  
Fluorescence Decay ◽  
Time Resolved Fluorescence ◽  
Time Resolved
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