Phosphorylation of synaptic-membrane proteins from ox cerebral cortex in vitro. Partition of substrates and protein kinase activities with triton X-100.
Synaptic-membrane fragments from ox cerebral cortex contain basal and cyclic AMP-stimulated protein kinase activity catalysing the phosphorylation of endogenous substrates. Extraction of membrane fragments with Triton X-100 solubilized less than 20% of the kinase activity and left the major part of the endogenous substrates in the insoluble fraction.
D000818:Animals; D002417:Cattle; D002540:Cerebral Cortex / Q000378:metabolism*; D000242:Cyclic AMP / Q000378:metabolism; D008297:Male; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D010750:Phosphoproteins / Q000096:biosynthesis*; D011494:Protein Kinases / Q000378:metabolism; D013570:Synaptic Membranes / Q000378:metabolism*
D009419:Nerve Tissue Proteins; D010750:Phosphoproteins; D000242:Cyclic AMP; D011494:Protein Kinases