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Phosphatidylcholine enhances the activity of rat liver type II phosphatidylinositol-kinase

  • H Olsson
  • Wilma Martinez Arias
  • Bengt Jergil
Publiceringsår: 1993
Språk: Engelska
Sidor: 332-6
Publikation/Tidskrift/Serie: FEBS Lett.
Volym: 327
Nummer: 3
Dokumenttyp: Artikel


A PtdIns 4-kinase was purified extensively from rat liver exocytotic vesicles. The enzyme had a low Km for ATP, was inhibited by adenosine, and had an apparent molecular mass of 54 kDa, indicating it to be a type II PtdIns-kinase. The activity of the purified enzyme was enhanced several-fold by PtdCho, and to some extent by other phospholipids with basic polar head groups, and was inhibited by PtdSer. Kinetic analyses, presenting the substrate in mixed micelles of Triton X-100, PtdIns and PtdCho, showed that the effect of PtdCho was both to increase Vmax and to decrease the apparent Km for micellar PtdIns.



  • Medicine and Health Sciences
  • Gel Enzyme Activation Exocytosis Liver/enzymology* Micelles Phosphatidylcholines/pharmacology* Phospholipids/pharmacology Phosphotransferases/isolation & purification Phosphotransferases/metabolism* Rats
  • 1-Phosphatidylinositol 4-Kinase Animals Chromatography



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