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Sensitive electrochemical detection of native and aggregated alpha-synuclein protein involved in Parkinson's disease
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SYSNO ASEP 0104692 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Ostatní články Title Sensitive electrochemical detection of native and aggregated alpha-synuclein protein involved in Parkinson's disease Title Elektrochemická analýza nativního a agregovaného alfa-synucleinu, proteinu, který se účastní na neurodegenerativních změnách vedoucích k Parkinsonově chorobě Author(s) Masařík, Michal (BFU-R)
Stobiecka, A. (PL)
Kizek, René (BFU-R)
Jelen, František (BFU-R) RID
Pechan, Zdeněk (BFU-R)
Hoyer, W. (DE)
Jovin, T. (DE)
Subramaniam, V. (DE)
Paleček, Emil (BFU-R) RID, ORCIDSource Title Electroanalysis. - : Wiley - ISSN 1040-0397
Roč. 16, 13-14 (2004), s. 1172-1181Number of pages 10 s. Language eng - English Country US - United States Keywords electrochemistry of proteins ; alpha-synuclein aggregation ; adsorptive transfer stripping Subject RIV BO - Biophysics R&D Projects GA204/03/0566 GA ČR - Czech Science Foundation (CSF) CEZ AV0Z5004920 - BFU-R Annotation The aggregation of alpha-synuclein, a 14 kDa protein, is involved in several human neurodegenerative disorders, including Parkinson's disease. We studied native and in vitro aggregated alpha-synuclein by circular dichroism (CD), atomic force microscopy (AFM) and electrochemical methods. We used constant current chronopotentiometric stripping analysis (CPSA) to measure hydrogen evolution catalyzed by alpha-synuclein (peak H) at hanging mercury drop electrodes (HMDE) and square-wave stripping voltammetry (SWSV) to monitor tyrosine oxidation at carbon paste electrodes (CPE). To decrease the volume of the analyte, most of the electrochemical measurements were performed by adsorptive transfer (medium exchange) from 3 - 6 muL drops of alpha-synuclein samples. Workplace Institute of Biophysics Contact Jana Poláková, polakova@ibp.cz, Tel.: 541 517 244 Year of Publishing 2005
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