Extraction of two different protein kinase activities from bovine rod outer segments.
An optimization of the rod outer segment (ROS) preparation technique is described. The protein responsible for ATP-gamma 32P 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.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D002417:Cattle; D002852:Chromatography, Ion Exchange; D000242:Cyclic AMP / Q000494:pharmacology; D006152:Cyclic GMP / Q000494:pharmacology; D004355:Drug Stability; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D010761:Phosphorus Radioisotopes; D010786:Photoreceptor Cells / Q000201:enzymology*; D011479:Protamines; D011494:Protein Kinases / Q000302:isolation & purification* / Q000378:metabolism; D012374:Rod Cell Outer Segment / Q000201:enzymology*
D010761:Phosphorus Radioisotopes; D011479:Protamines; D000255:Adenosine Triphosphate; D000242:Cyclic AMP; D011494:Protein Kinases; D006152:Cyclic GMP