Biochemistry (Moscow)

, Volume 70, Issue 12, pp 1341–1347 | Cite as

Functional Expression and Properties of Sec14p-Like Protein with Molecular Mass 45 kD from Rat Olfactory Epithelium

  • V. V. Radchenko
  • M. I. Merkulova
  • T. M. Shuvaeva
  • T. N. Simonova
  • A. A. Bondar
  • V. M. Lipkin


cDNA of Sec14p-like water-soluble protein with molecular mass 45 kD from rat olfactory epithelium was expressed in Escherichia coli Rosetta™ cells. The expression product was purified by a two-step chromatographic procedure on DEAE-Sepharose and Sephacryl S-200. The identity of structural and functional characteristics of the recombinant and native proteins was demonstrated by CD, mass spectrometry, and Western blotting. Using several lipids immobilized on nitrocellulose membranes, it was shown that phosphatidylinositol-3,4,5-triphosphate is the specific ligand for the studied protein.

Key words

lipid-binding protein p45 olfactory epithelium Sec14p family CRAL/TRIO domain protein—lipid interaction phosphatidylinositol-3,4,5-triphosphate 


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Copyright information

© MAIK "Nauka/Interperiodica" 2005

Authors and Affiliations

  • V. V. Radchenko
    • 1
  • M. I. Merkulova
    • 1
  • T. M. Shuvaeva
    • 1
  • T. N. Simonova
    • 1
  • A. A. Bondar
    • 2
  • V. M. Lipkin
    • 1
  1. 1.Shemyakin and Ovchinnikov Institute of Bioorganic ChemistryRussian Academy of SciencesMoscowRussia
  2. 2.Institute of Cell BiophysicsRussian Academy of SciencesPushchino, Moscow RegionRussia

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