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Related Experiment Videos

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
PubMed
Summary
This summary is machine-generated.

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AMP-deaminase from developing human placenta.

Placenta·2010

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.

Related Experiment Videos

  • 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.