PURIFICATION OF PROTHROMBIN AND THROMBIN BY CHROMATOGRAPHY ON CELLULOSE

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Abstract
A method is described for obtaining purified bovine thrombin by chromatography on phosphate cellulose, and purified bovine prothrombin by chromatography on diethylaminoethyl cellulose. Both proteins are obtained as single components, and in high yield. The purified prothrombin does not convert to thrombin in 25% sodium citrate solution or protamine sulphate solution. The N-terminal amino acid is the same as in purified prothrombin obtained by different methods in this laboratory, but instead of tyrosine and glycine the C-terminal amino acid is serine. A fundamental difference in structure is thus associated with altered activation characteristics.

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