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Human Prothrombin is a glycoprotein with a molecular weight of 70 kDa and is composed of a single polypeptide chain. Prothrombin is activated by factors Va, Xa, and phospholipids to produce the serine protease thrombin[1].

Prothrombin is purified by two absorptions on a barium citrate adsorbent, followed by decomposition of the adsorbents with a weak carboxylic cation-exchanger (Amberlite IRF-97), isoelectric precipitation (pH 4.7-4.9) and further purification by chromatography on Sephadex G-200 or IRC-50. Finally it is recrystallised from a 1% solution adjusted to pH 6.0-7.0 and partial lyophilisation to ca 1/5 to 1/10th volume and set aside at 2-5o to crystallise. Occasionally seeding is required. [Miller Biochemical Preparations 13 49 1971.]

[1] Suttie JW, et al. Prothrombin structure, activation, and biosynthesis. Physiol Rev. 1977 Jan;57(1):1-70. DOI:10.1152/physrev.1977.57.1.1