Extraction of two different protein kinase activities from bovine rod outer segments

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Abstract
An optimization of the rod outer segment (ROS) preparation technique is described. The protein responsible for ATP-γ32P binding to bovine ROS was separated from the protein active with protamine on a DEAE Sephadex column. Molecular weight evaluation on a G 100 Sephadex column gave a value of 75,000 for the protein active with ROS, and 42,000 for that active with protamine. 1.25 mM c-AMP or c-GMP reduced the activity to 0.7 or 0.8 of the control respectively. 10 mM c-GMP doubled the yield of the active protein extracted from ROS.