PURIFICATION AND SOME CHARACTERISTICS OF THE HUMAN COAGULATION FACTOR-VII

1. A purification procedure for factor VII (proconvertin) from human plasma is described. The procedure involves barium sulphate adsorption and elution, DEAE‐Sephadex column chromatography, barium sulphate adsorption and elution, heparin‐Sepharose column chromatography, preparative disc gel electrophoresis and finally adsorption with antiserum to prothrombin coupled to Sepharose and antiserum to albumin coupled to Sepharose. This procedure gave an approximately 8 · 105‐fold purification. 2. The factor VII obtained from the electrophoresis step was mainly a single‐chain protein with an apparent molecular weight of 53000 ± 2000. 3. After the final purification step, additional forms of factor VII, resulting from a fragmentation of the factor VII molecule were detected. 4. Amino acid composition data of the purified factor VII are given. 5. Antisera were raised in two different rabbits by injection of the purified factor VII. The antisera obtained gave a good titre against the factor VII activity and were not directed against any of the three other vitamin‐K‐dependent coagulation factors. Copyright © 1979, Wiley Blackwell. All rights reserved