Abstract
Summary
Highly purified thrombokinase, derived from bovine plasma, activated chymo-trypsinogen. Chymotrypsin was assayed by the hydrolysis of BTEE, which was not split by thrombokinase under the conditions used. Activation of chymotrypsinogen may have been due to thrombokinase, per se, or to an impurity, since a large quantity of thrombokinase was required. However, phosphatide accelerated the process, provided that ionic calcium was included. Without thrombokinase, phosphatide plus ionic calcium failed to activate chymotrypsinogen.
Much of the preparative work was done by William S. Bartek and Harriet F. Brown. We are indebted to Nadia Oulianoff for thrombokinase assays.
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