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Related Experiment Videos

[High purification of human thrombin]

J Zhong1, W Yin, Y Lin

  • 1Institute of Basic Medical Sciences, CRRC, Beijing.

Zhongguo Yi Xue Ke Xue Yuan Xue Bao. Acta Academiae Medicinae Sinicae
|February 1, 1995
PubMed
Summary

Researchers developed a method to highly purify human thrombin from plasma. This purified thrombin enzyme exhibits high specific activity and can be used in recombinant protein production.

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Area of Science:

  • Biochemistry
  • Protein Chemistry
  • Enzymology

Context:

  • Human plasma is a rich source of coagulation factors.
  • Thrombin plays a critical role in the coagulation cascade.
  • Efficient purification of active enzymes is essential for biochemical applications.

Purpose:

  • To develop a robust protocol for the purification of highly active human thrombin from plasma.
  • To characterize the purity and specific activity of the purified human thrombin.
  • To assess the utility of purified human thrombin as a tool enzyme in biotechnology.

Summary:

  • A purification strategy involving barium chloride adsorption, ammonium sulfate precipitation, and sequential chromatography (Amberlite and SP-Sephadex) was employed.
  • The resulting human thrombin preparation was homogeneous by SDS-PAGE, demonstrating a specific activity of 2000 NIH U/mg towards fibrinogen.
  • The overall recovery yield ranged from approximately 30% to 40%.

Impact:

  • Provides a reliable source of highly purified human thrombin for research and development.
  • Enables the use of thrombin as an effective tool enzyme in downstream processing of genetically engineered fused proteins.
  • Contributes to advancements in protein purification techniques and biotechnological applications.

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