Simplified electrophoretic separation of amyloid-ß peptides
ČlánekOtevřený přístuppeer-reviewedpublishedDatum publikování
2009
Vedoucí práce
Oponent
Název časopisu
Název svazku
Vydavatel
Univerzita Pardubice
Abstrakt
Several variants of amyloid-ß peptides, differing in their carboxy terminus, have been identified as the major component of cerebral deposits of amyloid found in the brains of patients with Alzheimer's disease. Recently, we have refined a simple and inexpensive method for analysis and separation of amyloid-ß peptides based on modification of discontinuous SDS-PAGE electrophoresis with utilization of Tricine as a trailing ion. Clear resolution was achieved by addition of high concentration of urea to the separation and stacking gel. The obtained data confirmed that described gel electrophoretic system is a superior procedure for the analysis of amyloid-ß peptides providing enhanced resolution even for peptides which differ only in few amino acids in the length of polypeptide chain.
Rozsah stran
p. 41-47
ISSN
1211-5541
Trvalý odkaz na tento záznam
Projekt
Zdrojový dokument
Scientific papers of the University of Pardubice.
Series A, Faculty of Chemical Technology. 13
(2007)
Vydavatelská verze
Přístup k e-verzi
Název akce
ISBN
Studijní obor
Studijní program
Signatura tištěné verze
47333
Umístění tištěné verze
Univerzitní knihovna (studovna)