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. 2002 May 15;22(10):3855–3863. doi: 10.1523/JNEUROSCI.22-10-03855.2002

Fig. 8.

Fig. 8.

dSlo-bound PKAc is catalytically active in vitro. Activity of PKAc was measured using the biotinylated Kemptide assay system. A, PKAc activity is not significantly different in reactions that contain PKAc alone (left), PKAc together with 5, 50, or 500 ng of either GST (right bars, n = 3) or the GST-dSlo fusion proteins (GST-A, middle bars, n = 3). B, PKAc activity is dramatically decreased in the presence of 5 ng of PKA regulatory subunit (RII, n = 3). Addition of 8.5 μg of either GST (RII + GST,n = 3) or GST-A fusion proteins (RII + GST-A, n = 3) does not significantly alter the inhibition of PKAc activity by RII.