Abstract
1. A normally occurring inhibitor (anti-XIa) of product XIa (contact product, activated PTA) was purified 100-fold by a combination of zinc acetate precipitation, anion exchange chromatography and starch block electrophoresis. 2. The inhibitor was shown by electrophoresis to have the mobility of an alpha globulin. The purified inhibitor was free of antithrombin III activity and anti-XIIa activity. The anti-XIa fraction was free of coagulation factor activity and was stable over a wide range of pH and temperature. Analytical ultracentrifugation of a purified inhibitor fraction showed a symmetrical peak of S20w = 3.69. 3. The inhibitor was not consumed during its interaction with product XIa. 4. With the use of the purified inhibitor, the product XIa preparation used was shown to be practically free of precursor factor XI or XII activity. * Present adress: College of Physicians and Surgeons, Columbia University, New York.
Funding Information
  • U.S. Public Health Service

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