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Pig prothrombin: purification and properties

F A Leone, G Chiericayo, J C Say

|January 1, 1976

Summary

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Highly purified pig prothrombin was prepared with a 776-fold increase in clotting activity. This study details the purification process and characterizes the resulting protein, providing insights into its properties and activation.

Area of Science:

Biochemistry
Protein Chemistry

Background:

Prothrombin is a crucial protein in the blood coagulation cascade.
Efficient purification methods are essential for studying prothrombin's structure and function.

Purpose of the Study:

To describe a procedure for obtaining highly purified pig prothrombin.
To characterize the biochemical properties of purified pig prothrombin.

Main Methods:

Multi-step purification protocol from pig plasma.
SDS-polyacrylamide gel electrophoresis for molecular weight determination.
Amino acid composition analysis and N-terminal/C-terminal residue identification.

Main Results:

Achieved a 776-fold purification of pig prothrombin with an 8% yield.

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Determined a molecular weight of 65,000 Da and specific activity of 1,460 NH units/mg.

Identified alanine as the sole N-terminal residue and serine as a C-terminal residue.

Conclusions:

The described method yields highly purified and active pig prothrombin.
Characterization provides a detailed profile of the purified protein.
Further investigation into the activation of purified prothrombin was conducted.