Phosphopeptide and phosphoprotein metabolism in brain.
Phosphopeptide and phosphoprotein phosphorylation was studied in rat brain microsomes and rat brain slices which were incubated in the presence of [gamma-32 P] ATP under various experimental conditions. Radioactive phosphoserine was isolated from phosphopeptides and phosphoproteins. Naplus, K+, Mg2+ and cyclic AMP had a stimulating effect on the labelling of phosphopeptides. Ouabain and Ca2+ lowered the level of 32P incorporation into the phosphopeptides. The phosphoproteins behaved similarly to the phosphopeptides except for the potassium effect. Chase experiments showed a faster decrease in the labelling of phosphopeptides than in phosphoproteins. We suggest that both compounds may be involved in active transport phenomena.
D000255:Adenosine Triphosphate / Q000378:metabolism*; D000818:Animals; D001693:Biological Transport, Active; D001921:Brain / Q000166:cytology / Q000187:drug effects; D002540:Cerebral Cortex / Q000378:metabolism*; D008861:Microsomes / Q000378:metabolism*; D009943:Organophosphorus Compounds / Q000378:metabolism; D010042:Ouabain / Q000494:pharmacology; D010085:Oxidative Phosphorylation; D010748:Phosphopeptides / Q000378:metabolism*; D010750:Phosphoproteins / Q000378:metabolism*; D010761:Phosphorus Radioisotopes; D051381:Rats; D012694:Serine / Q000378:metabolism
D009943:Organophosphorus Compounds; D010748:Phosphopeptides; D010750:Phosphoproteins; D010761:Phosphorus Radioisotopes; D012694:Serine; D010042:Ouabain; D000255:Adenosine Triphosphate