The Purification and Properties of an Abnormal Prothrombin Protein Produced by Dicumarol-treated Cows A COMPARISON TO NORMAL PROTHROMBIN

摘要: A physiologically inactive prothrombin protein has been purified from the plasma of dicumarol-treated cows to a high level purity. This gave 80% as much precipitation in an assay against bovine antibody did normal prothrombin. could be due difference antigenicity, or it reflection nonhomogeneity preparation. It was very similar its carbohydrate and amino acid composition, ability activated by several nonphysiological activators, molecular weight judged gel electrophoresis. Its disc electrophoretic pattern also showed little that unless calcium included buffers. Under these conditions apparent not bind same degree The other significant differences between two proteins are their physiological activity adsorption onto barium citrate precipitates. In every case abnormal failed have properties. appears three property this is result vitamin K action. That is, action required metabolic step which needed produce calcium-binding sites, necessary for responsible adsorption. These data suggest acts chemically altering some unknown fashion, attachment previously unrecognized prosthetic group.