Phosphatidylcholine enhances the activity of rat liver type II phosphatidylinositol-kinase
(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:
https://lup.lub.lu.se/record/1753801
- author
- Olsson, H ; Martinez Arias, Wilma LU and Jergil, Bengt LU
- organization
- publishing date
- 1993
- 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
- 2016-04-04 13:41:49
- date last changed
- 2021-01-03 06:28:07
@article{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}}, keywords = {{GelEnzyme ActivationExocytosisLiver/enzymology*MicellesPhosphatidylcholines/pharmacology*Phospholipids/pharmacologyPhosphotransferases/isolation & purificationPhosphotransferases/metabolism*Rats; 1-Phosphatidylinositol 4-KinaseAnimalsChromatography}}, language = {{eng}}, number = {{3}}, pages = {{6--332}}, publisher = {{Wiley-Blackwell}}, 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}}, doi = {{10.1016/0014-5793(93)81015-R}}, volume = {{327}}, year = {{1993}}, }