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Fig. 6. S-nitrosylated parkin (SNO-PARK) was detected in brain tissue from Parkinson’s disease (PD) patients with diffuse Lewy body disease but not in postmortem samples from patients with other neurological disorders. Two PD patient samples (different from those shown in Fig. 3C) were positive for SNO-PARK by the biotin-switch assay on the same blot that had negative controls from two samples of Huntington’s disease (HD) and two samples of Alzheimer’s disease (AD).

Fig. 7. Partial liquid chromatography (LC) quadrupole time-of-flight (Q-TOF) MS spectra of recombinant GST-parkin after S-nitrosocysteine (SNOC) exposure (A, C, E, and G) or control (B, D, F, and H). These spectra were obtained by combining a broad range of retention times (Rt) in the chromatograms, whereas the inserts were obtained from a narrow range of Rt to demonstrate the m/z values, the charge states, and the relative intensities of the peaks of interest. (A and B) Rt range, 32.0-40.0 min; m/z range, 600-700. Inserts constructed from Rt 32.8-33.8 min. (C and D) Rt range 69.5-74.5 min; m/z range 770-870. Inserts from Rt 70.5-71.5 min. (E and F) Rt range 87.7-89.5 min; m/z range 1020-1120. Inserts from Rt 88.0-89.0 min. (G and H) Rt range 74.5-82.5 min; m/z range 840-940. Inserts from Rt 77.0-78.0 min. Peaks labeled with asterisks were identified tryptic peptides of parkin that lacked nitrosylated, sulfinated, or sulfonated cysteine residues.

Summary of Q-TOF MS data for recombinant GST-parkin exposed to SNOC. Tryptic peptides with modifications of Cys-SNO, Cys-SNO_2, Cys-SOH, Cys-SO₂H, or Cys-SO₃H were identified in the RING I, In-Between RING, and RING II domains of parkin. The amino acid sequences, observed and calculated masses, and cysteine residue modifications of these peptides are listed.