The state of phosphorylation in vivo of membrane-bound phosphoproteins in rat brain.
The alkali-labile P content of membrane protein prepared from rapidly frozen rat brain was measured, CuSO(4) being used to inhibit protein phosphatase activity during subcellular fractionation. The P content of the membrane fraction was significantly increased (+12%) over the control value by incubation of homogenates with ATP before fractionation. This suggests that the membrane protein in rat brain is normally only partially phosphorylated.
D000818:Animals; D001921:Brain / Q000166:cytology; D001923:Brain Chemistry; D003300:Copper; D006863:Hydrogen-Ion Concentration; D010750:Phosphoproteins / Q000032:analysis*; D010756:Phosphoric Acids / Q000032:analysis*; D010759:Phosphorus Isotopes; D051381:Rats; D013347:Subcellular Fractions / Q000032:analysis
D010750:Phosphoproteins; D010756:Phosphoric Acids; D010759:Phosphorus Isotopes; D003300:Copper