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. 1998 Nov;153(5):1365–1370. doi: 10.1016/s0002-9440(10)65722-7

Figure 2.

Figure 2.

Western blot analysis performed with MAb LB509 demonstrated high molecular mass aggregates of α-synuclein in the amygdala from FAD patients with PS-1 mutations. Amygdalas from control and FAD patients were fractionated as described in Materials and Methods. A: α-Synuclein in the high-salt-soluble fractions from the amygdala of three FAD cases (FAD1-3) compared with the amygdala from two control cases (C1-2). B: α-Synuclein in the high-salt-insoluble, Triton X-100-soluble fractions. C: α-Synuclein in formic-acid-extractable fractions. Five microliters of high-salt-insoluble, Triton X-100-soluble extracts or 10 μl of formic-acid-extractable extracts was loaded in each lane, respectively. The Western blots developed from high-salt-soluble and Triton X-100-soluble extracts were exposed to film for the same length of time, whereas the blot developed from formic-acid-extractable samples was exposed approximately five times longer.