Immunoblots of nitrosocysteine. Skeletal SR vesicles (lanes 1–4, 10
μg each lane) and cell membrane fractions containing C3635A RyR1
(lanes 5–8, 40 μg each lane) or wt-RyR1 (lanes 9–12, 40 μg each
lane) were incubated for 1 hr at 24°C in pO2 ≈ 10
mmHg or pO2 ≈ 150 mmHg in the presence of 1 μM NO.
Anti-nitrosocysteine negative controls (treated with 0.1
mmHgCl2, odd-numbered lanes), samples without NO (lanes 2,
6, and 10), and samples treated with 1 μM NO (lanes 3 and 4, 7 and 8,
11 and 12) at pO2 ≈ 10 mmHg (B) and
pO2 ≈ 150 mmHg (C) were separated by
SDS/3–12% PAGE gradient. The proteins were transferred to
Immobilon-P membranes overnight at 4°C. A polyclonal
anti-nitrosocysteine antibody was used to detect an S-nitrosylation
signal in the protein band region of RyR1 probed with D110 monoclonal
anti-RyR1 (A). The data are representative of three
experiments.