Detection, Purification and Identification of An Endogenous Inhibitor of l-Dopa Decarboxylase Activity from Human Placenta |
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Authors: | Alice-Georgia Vassiliou Emmanuel G Fragoulis Dido Vassilacopoulou |
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Institution: | (1) Department of Biochemistry and Molecular Biology, University of Athens, Panepistimiopolis, Zografou, 15701 Athens, Greece |
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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. |
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Keywords: | Ddc Membrane Activity inhibitor Annexin V Placenta |
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