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Sheep prothrombin: purification and partial characterization

G Chiericato, J C Say, F A Leone

    Biochimica Et Biophysica Acta
    |December 22, 1976
    PubMed
    Summary
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    Highly purified sheep prothrombin was prepared and characterized. This research details the isolation and properties of sheep prothrombin, a key clotting factor.

    Area of Science:

    • Biochemistry
    • Hematology

    Background:

    • Prothrombin is a crucial precursor to thrombin in the blood coagulation cascade.
    • Understanding prothrombin's properties is essential for studying hemostasis and thrombosis.

    Purpose of the Study:

    • To describe a method for obtaining highly purified sheep prothrombin.
    • To characterize the biochemical and biophysical properties of purified sheep prothrombin.

    Main Methods:

    • Disc gel electrophoresis in polyacrylamide for purity assessment.
    • Isoelectric focusing for isoelectric point determination.
    • Amino acid analysis and SDS-polyacrylamide gel electrophoresis for molecular weight and composition.

    Main Results:

    • Purified sheep prothrombin yielded a single band on electrophoresis, indicating high purity.

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  • Alanine was identified as the N-terminal residue, with no C-terminal residue released by carboxypeptidases.
  • The isoelectric point was determined to be 4.9-5.0.
  • Molecular weight was estimated at approximately 66,000 (amino acids) and 77,000 (including carbohydrates).

    • Conclusions:

    • A reliable method for preparing pure sheep prothrombin was established.
    • The characterized properties provide a basis for further functional studies of sheep prothrombin.
    • The data contribute to the understanding of mammalian prothrombin structure and function.