Related Experiment Video
Updated: Aug 12, 2026
05:31
Isolation, Cryopreservation and Culture of Human Amnion Epithelial Cells for Clinical Applications
Published on: December 21, 2014
AMP-deaminase from human term placenta
A Swieca1, I Rybakowska, G Nagel-Starczynowska
1Department of Biochemistry, Medical University of Gdansk, Gdansk, Poland.
Molecular and Cellular Biochemistry
|October 28, 2003
Summary
Human term placenta AMP-deaminase exhibits sigmoid kinetics and is regulated by allosteric effectors. This enzyme shares properties with liver AMP-deaminase, indicating its presence in placental tissue.
Area of Science:
- Biochemistry
- Enzymology
Background:
- AMP-deaminase is a crucial enzyme in purine metabolism.
- Understanding its properties in different tissues is important for metabolic research.
Purpose of the Study:
- To purify and characterize AMP-deaminase from human term placenta.
- To investigate its kinetic and immunological properties.
Main Methods:
- Phosphocellulose column chromatography for enzyme purification.
- Enzyme kinetics assays under various effector conditions.
- SDS-PAGE electrophoresis and immunological analysis.
Main Results:
- Purified placental AMP-deaminase showed sigmoid substrate saturation kinetics (S0.5 ≈ 7 mM).
- Allosteric effectors (ATP, ADP, orthophosphate) modulated enzyme kinetics.
- Stearylo-CoA potently inhibited the enzyme.
- SDS-PAGE revealed a 68 kDa fragment reactive with anti-liver AMP-deaminase antibodies.
Conclusions:
- Human term placenta contains a 'liver type' AMP-deaminase.
- The enzyme exhibits complex allosteric regulation and specific inhibition patterns.
