Zobrazit minimální záznam
dc.contributor.author |
Zdražilová, Pavla
|
|
dc.contributor.author |
Holub, Dušan
|
|
dc.contributor.author |
Bílková, Zuzana
|
|
dc.date.accessioned |
2009-06-19T08:42:28Z |
|
dc.date.available |
2009-06-19T08:42:28Z |
|
dc.date.issued |
2009 |
|
dc.identifier |
Univerzitní knihovna (studovna) |
cze |
dc.identifier.issn |
1211-5541 |
|
dc.identifier.uri |
http://hdl.handle.net/10195/32931 |
|
dc.description.abstract |
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. |
eng |
dc.format |
p. 41-47 |
cze |
dc.language.iso |
eng |
|
dc.publisher |
Univerzita Pardubice |
cze |
dc.relation.ispartof |
Scientific papers of the University of Pardubice.
Series A, Faculty of Chemical Technology. 13
(2007) |
eng |
dc.title |
Simplified electrophoretic separation of amyloid-ß peptides |
eng |
dc.type |
article |
cze |
dc.identifier.signature |
47333 |
|
dc.peerreviewed |
yes |
eng |
dc.publicationstatus |
published |
eng |
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