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. 1978 Apr 12;523(2):494-505.
doi: 10.1016/0005-2744(78)90052-9.

In vitro prothrombin synthesis from a purified precursor protein. II. Partial purification of bovine carboxylase

In vitro prothrombin synthesis from a purified precursor protein. II. Partial purification of bovine carboxylase

C Vermeer et al. Biochim Biophys Acta. .

Abstract

In this paper, we describe the isolation and partial purification of an enzyme system that converts bovine decarboxyfactor II (PIVKA-II) into prothrombin (factor II). It is shown that the increase in factor II activity occurs in parallel with 14CO2 incorporation into BaSO4 adsorbable proteins. The system is not strictly vitamin K-dependent because it is obtained from the livers of normal healthy cows. By preincubating the enzyme(s) with an excess of warfarin, an absolute vitamin K1-dependence can be obtained. The reaction is inhibited by its own product, factor II.

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