These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Characterization of phosphatidylinositol-4-phosphate 5-kinase activities from bovine brain membranes.
    Author: Moritz A, Westerman J, De Graan PN, Payrastre B, Gispen WH, Wirtz KW.
    Journal: Biochim Biophys Acta; 1993 May 20; 1168(1):79-86. PubMed ID: 8389203.
    Abstract:
    Phosphatidylinositol-4-phosphate (PtdIns(4)P) kinase activity associated with bovine brain membranes, was released by NaCl treatment and partially purified by chromatography on phosphocellulose, phenylsepharose, Ultrogel AcA44, DEAE-cellulose and ATP-agarose. The final preparation contained a 6333-fold purified protein fraction with a specific activity of 171 nmol.min-1 x mg-1. Under conditions where this PtdIns(4)P kinase activity (PtdIns(4)P kinase activity b) did not bind to DEAE-cellulose, a PtdIns(4)P kinase activity purified earlier (Moritz, A., De Graan, P.N.E., Ekhart, P.F., Gispen, W.H. and Wirtz, K.W.A. (1990) J. Neurochem. 54, 351-354) does bind (PtdIns(4)P kinase activity a). Both enzyme activities specifically used PtdIns(4)P as substrate and phosphorylated the inositol moiety at the 5'-position. PtdIns(4) kinase activity a has an apparent Km of 18 microM for PtdIns(4)P whereas PtdIns(4)P kinase activity b has a Km of 4 microM. All other measured kinetic parameters (i.e., Km for ATP, Mg(2+)-dependence, pH optimum, activation by phosphatidylserine and inhibition by phosphatidylinositol 4,5-bisphosphate) were similar for both enzyme activities.
    [Abstract] [Full Text] [Related] [New Search]