In vitro prothrombin synthesis from a purified precursor protein. II. Partial purification of bovine carboxylase.
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.
D000818:Animals; D002262:Carboxy-Lyases / Q000302:isolation & purification / Q000378:metabolism*; D002417:Cattle; D005260:Female; D007700:Kinetics; D008862:Microsomes, Liver / Q000201:enzymology; D010100:Oxygen; D011516:Prothrombin / Q000096:biosynthesis*; D014812:Vitamin K / Q000494:pharmacology; D014859:Warfarin / Q000494:pharmacology
D014812:Vitamin K; D014859:Warfarin; D011516:Prothrombin; D002262:Carboxy-Lyases; D010100:Oxygen