Protein histidine phosphatase activity in rat liver and spinach leaves.
Whole cell extracts from rat liver or spinach leaves contain divalent ion-independent protein histidine phosphatase activity due to phosphatases of the PP1/PP2A family. In the rat liver extract, almost all the activity was found in the PP1, PP2A1 and PP2A2 peaks. In the spinach leaf extract, four phosphorylase phosphatase activity peaks were resolved--three containing PP1 and one containing PP2A--and all showed histidine phosphatase activity. Thus, protein histidine phosphatase activity is expressed in the cytosolic forms of protein phosphatases of the PP1/PP2A family in mammalian and plant cells.
Matthews
H R
HR
Biochemistry Department, The University, Dundee, UK.
MacKintosh
C
C
D000818:Animals; D003600:Cytosol / Q000201:enzymology; D006639:Histidine / Q000031:analogs & derivatives* / Q000378:metabolism; D008099:Liver / Q000201:enzymology; D010749:Phosphoprotein Phosphatases / Q000302:isolation & purification / Q000378:metabolism*; D018515:Plant Leaves / Q000201:enzymology; D051381:Rats; D018724:Spinacia oleracea / Q000201:enzymology
D006639:Histidine; D010749:Phosphoprotein Phosphatases; C005436:phosphohistidine