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. 2011 Feb 17;286(16):14168–14177. doi: 10.1074/jbc.M111.222430

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© 2011 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 3. — Mass spectrometric analysis of peptides generated from both WT and mutants form of α-synuclein by cMMP3 cleavage. A, after 30 min of incubation with cMMP3 (1 μg/ml), peptides from WTsyn, A30Psyn, and A53Tsyn (1 μg each) were analyzed by Fourier transform-ion cyclotron resonance mass spectrometry. Blue ovals represent two strong peaks generated exclusively in A53Tsyn. B, amino acid sequences and intensity determined accordingly with deconvoluted m/z values and N-terminal amino acids. Note that band a consists of two peptides (1–93 and 1–91 aa), and band b also consists of two (1–79 and 1–78 aa). Band c is one peptide of 1–47 aa, which is exclusively generated from A53T.