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

In English

Författare

  • H Olsson
  • Wilma Martinez Arias
  • Bengt Jergil

Summary, in English

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.

Publiceringsår

1993

Språk

Engelska

Sidor

6-332

Publikation/Tidskrift/Serie

FEBS Letters

Volym

327

Issue

3

Dokumenttyp

Artikel i tidskrift

Förlag

Wiley-Blackwell

Ämne

  • Basic Medicine

Nyckelord

  • GelEnzyme ActivationExocytosisLiver/enzymology*MicellesPhosphatidylcholines/pharmacology*Phospholipids/pharmacologyPhosphotransferases/isolation & purificationPhosphotransferases/metabolism*Rats
  • 1-Phosphatidylinositol 4-KinaseAnimalsChromatography

Status

Published

ISBN/ISSN/Övrigt

  • ISSN: 1873-3468