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Related Experiment Videos

Human plasma gelsolin binds adenosine triphosphate.

H Yamamoto1, H Ito, H Nakamura

  • 1Third Department of Internal Medicine, Osaka University School of Medicine.

Journal of Biochemistry
|October 1, 1990
PubMed
Summary
This summary is machine-generated.

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Human plasma gelsolin binds ATP with a high affinity, featuring one binding site per molecule. This finding clarifies the interaction between gelsolin and adenosine triphosphate (ATP) in biological systems.

Area of Science:

  • Biochemistry
  • Molecular Biology

Background:

  • Plasma gelsolin is a crucial protein involved in actin dynamics.
  • Understanding its interaction with nucleotides like ATP is essential for elucidating its cellular functions.

Purpose of the Study:

  • To investigate the binding characteristics of human plasma gelsolin with adenosine triphosphate (ATP).
  • To determine the affinity and stoichiometry of ATP binding to plasma gelsolin.

Main Methods:

  • Equilibrium dialysis was employed to study the binding of human plasma gelsolin with ATP.
  • Bioluminescent assays using luciferin and firefly luciferase were utilized to confirm nucleotide presence.

Main Results:

  • Plasma gelsolin exhibits one class of ATP binding site.

Related Experiment Videos

  • The dissociation constant (Kd) for ATP binding was determined to be 2.8 x 10(-7) M.
  • Binding saturation occurred at an ATP/gelsolin ratio of 0.6, indicating a specific stoichiometry.

    • Conclusions:

    • Human plasma gelsolin possesses a high-affinity ATP binding site.
    • The results provide quantitative insights into the molecular interaction between gelsolin and ATP.