Abstract
Summary
Thrombokinase 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 production of thrombin in a system containing prothrombin, cephalin, calcium 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 thrombin and thrombokinase peaks.
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