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To confirm that multiple forms of prothrombin are induced by dicoumarol, we isolated prothrombins from the plasma of dicoumarol-treated steers and divided them into three groups: 1) barium (Ba) citrate variant adsorbable by Ba citrate; 2) Ba oxalate material adsorbable by Ba oxalate but not by Ba citrate; and 3) the alumina atypical proteins(s) adsorbable by alumina Cγ-gel but not by the Ba salts. The purified atypical varieties showed a single component by several physicochemical criteria and contained as much antigenic material as did normal prothrombins, but bound different amounts of Ca2+. The Ca2+-binding ability of these proteins depends on the carboxylation of the glutamyl residues on the amino portion of prothrombin. The extra car-boxyl groups appeared to have little influence on the isoelectric points of prothrombins because the Ba citrate variant binding Ca2+, equal to 38% of the normal, focused at the same pH (pH 4.55 or 4.6) as normal prothrombin. Ba oxalate proteins bound Ca2+ equal to 25% of normal and focused at pH 4.75; the alumina variant(s) bound little, if any Ca2+ and focused at pH 4.82. To prove unequivocally whether or not multiple forms of dicoumarol-induced prothrombins are produced, normal and atypical prothrombins were digested separately with thrombin to yield Fragment 1 (F1) and Intermediate 1 (II). Both F1 and I1 were obtained in highly purified forms by employing DEAE-cellulose chromatography, gel-filtration, and affinity chromatography on heparin-agarose. Since the Ca2+ binding sites reside in Fl, they were characterized (Ca2+-binding abilities, electrophoretic mobilities, antigenic properties and gel-isoelectrofocusing). In general, these experiments confirmed our studies with intact proteins: i.e., that different forms of atypical prothrombins are induced by dicoumarol and they differ from each other primarily in the extent of carboxylation of the glutamyl residues present in the amino portion of prothrombin.

Characterization of Multiple forms of Dicoumarol-Induced Prothrombins and Their Fragments, F1