Abstract
Bovine thrombin has been purified from commercial crude thrombin preparations by affinity chromatography on immobilized heparin. This procedure was shown to be superior to affinity chromatography on matrix-linked synthetic low-molecular-weight thrombin inhibitors in that the purified enzyme could be conveniently eluted by a salt gradient and also was of higher purity. The degree of purification of the affinity chromatography step was 30 times and the purified material had a specific activity of about 2000 NIH units/mg. Dodecyl sulphate-polyacrylamide gel electrophoresis indicated the presence of the native two-chain form of thrombin as well as of several forms of thrombin with specific proteolytic cleavages in the B-chain. These modified forms were similar to those also found in thrombin preparations obtained from crude commercial thrombin by other methods. Affinity chromatography on heparin-agarose was shown to be useful also for the purification of thrombin from a prothrombin activation mixture.
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