Abstract
Prothrombin was identified in rat liver microsomal extracts by its biological activity, adsorption on BaSO 4, and electrophoretic mobility. The prothrombin activity was very low in normal rats and absent in vitamin K-deficient rats or rats treated with warfarin. Liver prothrombin concentrations in those rats reached a maximum 10 or 15 min after vitamin K administration, and then fell as prothrombin was secreted into the plasma. The appearance of prothrombin in the liver is not blocked by administration of sufficient cycloheximide to block liver protein synthesis. These data provide additional evidence that the function of vitamin K is to activate a preformed liver precursor to active prothrombin.
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