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Related Experiment Videos

Kringle domains and plasmin denaturation.

G Y Shi1, D H Wu, H L Wu

  • 1Biochemistry Department, Medical College, National Cheng-Kung University, Tainan, Taiwan, Republic of China.

Biochemical and Biophysical Research Communications
|July 15, 1991
PubMed
Summary

Fibrinogen degradation products (FDP) accelerate plasmin denaturation, particularly affecting Lys-plasmin and mini-plasmin. FDP also influences plasminogen oligomerization, with effects varying by concentration.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Chemistry

Background:

  • Plasmin plays a crucial role in fibrinolysis.
  • Understanding plasmin stability and interactions is vital for thrombolytic therapies.
  • Fibrinogen degradation products (FDP) are generated during clot breakdown.

Purpose of the Study:

  • To investigate the effect of FDP on plasmin denaturation rates.
  • To explore the influence of FDP on plasminogen oligomerization and interactions.

Main Methods:

  • Assessing plasmin denaturation rates using different plasmin forms (Lys-plasmin, miniplasmin, microplasmin).
  • Quantifying FDP-induced changes in denaturation kinetics.
  • Analyzing plasminogen oligomer formation using cross-linking and SDS-PAGE.

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Main Results:

  • Denaturation rates followed the order: Lys-plasmin > miniplasmin > microplasmin.
  • FDP dose-dependently increased denaturation rates of Lys-plasmin and mini-plasmin.
  • FDP affected plasminogen oligomerization, with low concentrations promoting oligomer formation and high concentrations decreasing it.
  • FDP's effect on plasmin denaturation correlated with its impact on kringle domain interactions.

Conclusions:

  • FDP significantly modulates plasmin stability and denaturation.
  • FDP influences the aggregation state of plasminogen, impacting its interactions.
  • These findings provide insights into the complex interplay between fibrinolysis components.