Separation of Thrombin from Thrombokinase by Continuous Flow Paper Electrophoresis.

Abstract

Thrombokinase which had been prepared from bovine plasma was further purified by continuous flow paper electrophoresis. Thrombokinase was assayed by its capacity to activate prothrombin in the presence of oxalate, and also by the production of thrombin in a system containing prothrombin, cephalin, Ca and bovine "barium carbonate serum". Curves of these 2 assays were similar and formed a peak ahead of the thrombin peak. TAMe esterase activity appeared in 2 peaks which corresponded, respectively, to the thrombin and thrombokinase peaks.