Abstract
Summary
The electrophoretic mobility of bovine prothrombin is greater than that of the more concentrated plasma protein constituents. At pH 7, heparin does not alter the mobility of prothrombin. The isoelectric point of prothrombin is in the region of pH 4.8 and in all probability is identical with the inactivation point. It is estimated that pure prothrombin will posses, 1,300 to 1,500 units activity per mg of protein.
We wish to thank Miss Ann Garrett for technical assistance.
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