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. Author manuscript; available in PMC: 2013 May 14.
Published in final edited form as: Biochemistry. 2008 Dec 23;47(51):10.1021/bi801024a. doi: 10.1021/bi801024a

Fig. 6.

Fig. 6

Dephosphorylation of SERCA1 by ADP after 10, 116 and 223 ms of phosphorylation at 2°C and 0.4 M KCl. SERCA1 in sealed SR vesicles (.375 mg/ml) suspended in standard buffer containing 0.4 M KCl, was phosphorylated by 100 µM [γ32P]ATP at 2°C. After 10 ms (filled circles), 116 ms (filled diamonds), or 223 ms (filled squares), a chase containing 1.66 mM ADP was added to dephosphorylate the enzyme and the reaction allowed to proceed for the indicated times before quenching with acid (see Materials and Methods). Dashed line approximates the time course of phosphorylation (filled squares) in Fig. 5. Inset shows the time course of dephosphorylation produced by chasing with 1.66 mM ADP 30 s after the start of phosphorylation. Brackets indicate the amount of E1P and E2P revealed by chasing with ADP after 116 ms of phosphorylation.