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.
