Formation of amyloid oligomers by AChE<sub>586-599</sub> and AChE<sub>586-599</sub> mutants.

<p>Oligomers of AChE<sub>586-599</sub> and AChE<sub>586-599</sub> mutants (12 µM) were cross-linked by photo-induced cross-linking. Cross-linked products were resolved (16.5% Tris-Tricine SDS-PAGE), electro-blotted onto nitrocellulose and probed with Mab 105A (specific for AChE<sub>586-599</sub> in β-sheet conformation). Marker proteins are indicated. Arrows indicate low abundance oligomeric species. Due to the strength of the signal for the oligomeric species, Y<sub>9</sub>/A was loaded at a third of the amount of the other peptides (Y<sub>9</sub>/A*). The signal resulting from loading equal amount to the other peptides can be seen on the individual lane on the right hand side of the top panel (Y<sub>9</sub>/A). On the right hand side of the bottom panel, an overexposure of the signal for W<sub>13</sub>/A shows multiple oligomeric species not seen at normal exposure.</p>

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