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Bovine vitamin K-dependent carboxylase was prepared, both from normal cows and from warfarin-treated ones. The two carboxylating enzyme systems were similar except for the fact that carboxylase from warfarin-treated cows contained a 100-fold higher amount of endogenous substrate. About 65% of this substrate consisted of one-chain factor X-precursor (s) and 25% of prothrombin-precursor(s). Solubilized carboxylase could be purified more than 100-fold by immuno- specific adsorption onto immobilized antifactor X antibodies. The purified enzyme contained 40% (w/w) phospholipid (mainly phosphatidylcholine), which was absolutely required for the carboxylating activity.  Carboxylase from non-anticoagulated cows was used for studying exogenous substrates. Bovine descarboxyprothrombin, descarboxyfragment-1 and the pentapeptide Phe-Leu-Glu- Glu-Leu were carboxylated with a low efficiency (Km, between 0.4 and 11 mM). On the other hand a peptide, identical to the amino acid residues 13-29 in descarboxyprothrombin, had a Km of 0.001 mM. It seems probable therefore that the latter peptide contains all information required for a good substrate.

The Carboxylation Of Bovine Vitamin K-Dependent Proteins By Bovine Carboxylase