Platelet phosphoprotein phosphatase activity. Its subcellular distribution and regulation.
Phosphoprotein phosphatase (EC 3.1.3.-) activity was found in human platelet homogenates and this activity was stimulated up to 20-fold by preincubation with trypsin. Both Mg2+ and Mn2+ greatly decreased the activity of trypsin-activated phosphatase but the activity of the untreated phosphatase was not affected by increasing the concentration of these divalent cations. It was also shown that the activity of the phosphatase underwent a transient inhibition upon addition of ATP and a permanent one with ATP-gamma-S.
D000255:Adenosine Triphosphate / Q000031:analogs & derivatives / Q000494:pharmacology; D001792:Blood Platelets / Q000201:enzymology*; D006801:Humans; D008274:Magnesium / Q000494:pharmacology; D008345:Manganese / Q000494:pharmacology; D010749:Phosphoprotein Phosphatases / Q000097:blood*; D010765:Phosphorylase Phosphatase / Q000037:antagonists & inhibitors / Q000097:blood*; D013347:Subcellular Fractions / Q000201:enzymology; D013873:Thionucleotides / Q000494:pharmacology; D014357:Trypsin / Q000494:pharmacology
D013873:Thionucleotides; C022571:adenosine 5'-O-(3-thiotriphosphate); D008345:Manganese; D000255:Adenosine Triphosphate; D010749:Phosphoprotein Phosphatases; D010765:Phosphorylase Phosphatase; D014357:Trypsin; D008274:Magnesium