Neurochemical Research

, Volume 34, Issue 6, pp 1089–1100

Detection, Purification and Identification of An Endogenous Inhibitor of l-Dopa Decarboxylase Activity from Human Placenta

  • Alice-Georgia Vassiliou
  • Emmanuel G. Fragoulis
  • Dido Vassilacopoulou
ORIGINAL PAPER

DOI: 10.1007/s11064-008-9879-2

Cite this article as:
Vassiliou, AG., Fragoulis, E.G. & Vassilacopoulou, D. Neurochem Res (2009) 34: 1089. doi:10.1007/s11064-008-9879-2

Abstract

An endogenous inhibitor of l-Dopa decarboxylase activity was identified and purified from human placenta. The endogenous inhibitor of l-Dopa decarboxylase (Ddc) was localized in the membrane fraction of placental tissue. Treatment of membranes with phosphatidylinositol-specific phospholipase C or proteinase K did not affect membrane-associated Ddc inhibitory activity, suggesting that a population of the inhibitor is embedded within membranes. Purification was achieved by extraction from a nondenaturing polyacrylamide gel. The purification scheme resulted in the isolation of a single 35 kDa band, bearing l-Dopa decarboxylase inhibitory activity. The purified inhibitor was identified as Annexin V. The elucidation of the biological importance of the presence of an l-Dopa decarboxylase activity inhibitor in normal human tissues could provide us with new information leading to the better understanding of the biological pathways that Ddc is involved in.

Keywords

Ddc Membrane Activity inhibitor Annexin V Placenta 

Copyright information

© Springer Science+Business Media, LLC 2008

Authors and Affiliations

  • Alice-Georgia Vassiliou
    • 1
  • Emmanuel G. Fragoulis
    • 1
  • Dido Vassilacopoulou
    • 1
  1. 1.Department of Biochemistry and Molecular BiologyUniversity of AthensAthensGreece

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