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

Olsson, H; Martinez Arias, Wilma LU and Jergil, Bengt LU (1993) In FEBS Letters 327(3). p.6-332
Abstract
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.
Please use this url to cite or link to this publication:
author
organization
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type
Contribution to journal
publication status
published
subject
keywords
GelEnzyme ActivationExocytosisLiver/enzymology*MicellesPhosphatidylcholines/pharmacology*Phospholipids/pharmacologyPhosphotransferases/isolation & purificationPhosphotransferases/metabolism*Rats, 1-Phosphatidylinositol 4-KinaseAnimalsChromatography
in
FEBS Letters
volume
327
issue
3
pages
6 - 332
publisher
Wiley-Blackwell
external identifiers
  • Scopus:0027257154
ISSN
1873-3468
DOI
10.1016/0014-5793(93)81015-R
language
English
LU publication?
yes
id
9edd2356-3fdc-4e30-8a43-c08e8564ef28 (old id 1753801)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/8394247
date added to LUP
2010-12-29 11:05:56
date last changed
2016-11-17 15:33:23
@misc{9edd2356-3fdc-4e30-8a43-c08e8564ef28,
  abstract     = {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.},
  author       = {Olsson, H and Martinez Arias, Wilma and Jergil, Bengt},
  issn         = {1873-3468},
  keyword      = {GelEnzyme ActivationExocytosisLiver/enzymology*MicellesPhosphatidylcholines/pharmacology*Phospholipids/pharmacologyPhosphotransferases/isolation & purificationPhosphotransferases/metabolism*Rats,1-Phosphatidylinositol 4-KinaseAnimalsChromatography},
  language     = {eng},
  number       = {3},
  pages        = {6--332},
  publisher    = {ARRAY(0x79cd010)},
  series       = {FEBS Letters},
  title        = {Phosphatidylcholine enhances the activity of rat liver type II phosphatidylinositol-kinase},
  url          = {http://dx.doi.org/10.1016/0014-5793(93)81015-R},
  volume       = {327},
  year         = {1993},
}