Modified Method for the Preparation of Purified Bovine Prothrombin of High Specific Activity

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Abstract
A modified method for the isolation and purification of bovine prothrombin is described. The preparations have a very high specific activity, viz. 3,200 ± 200 u/mg of protein, show a single symmetrical peak in the analytical ultracentrifuge and by moving boundary electrophoresis at both pH 6.86 and 8.6. They do not undergo inactivation or dissociation during electrophoresis at high voltage gradient (7.5) at alkaline pH. Disc electrophoresis also shows essentially a single component. For optimal activation, prothrombin requires the presence of factor VII-X complex in addition to factor V. * This work was supported in part by U. S. Public Health Service Grant HE 10571 (formerly AM 04847). ** Present address: Veterans Administration Hostpital, Cleveland, Ohio. *** Present address : Institute of Pathology, Western Reserve University, Cleveland, Ohio.

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