Phosphorylation of caesin by ROS soluble fraction and the cGMP-gated channel by a human recombinant CK2 A. The ability of a soluble fraction from ROS to phosphorylate bovine milk casein was examined by autoradiography. lane a: casein alone; lane b: casein phosphorylated using a hypotonic soluble fraction from ROS; lane c: casein phosphorylated using a diluted (1:30) ROS soluble fraction; lane d: casein phosphorylated using ROS lysate depleted of CK2 by immunoprecipitation; lane e: phosphorylated ROS lysate. B. Phosphorylation of the rod channel by recombinant CK2. Washed ROS membranes were solubilized in CHAPS and the cGMP-gated channel bound to PMc 1D1-Sepharose. The bound channel complex was phosphorylated in the presence of CHAPS detergent by the addition of exogenous CK2 (2.3 U), eluted from the column and subjected to SDS gel electrophoresis. Phosphorylation of the channel was detected by autoradiography. lane a: purified channel incubated with [γ-32P]ATP; lane b: purified channel incubated with exogenous CK2 and [γ-32P]ATP.
From: Regulation of the Rod Photoreceptor Cyclic Nucleotide-Gated Channel
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