INTERACTION OF BOVINE AUTOPROTHROMBIN C WITH PHOSPHOLIPIDS AND DIVALENT CATIONS,
Abstract
A thromboplastic enzyme, autoprothrombin C, can be complexed to different phospholipids and removed from solution in the form of such complexes. A technique for dissociating these complexes was developed, resulting in the recovery of the thromboplastic enzyme essentially free of phospholipid and in a higher degree of purity. Calcium ions are required for the formation of the complex, but strontium can replace calcium not only as the metal ion in the phospholipid-complexing system, but also as an autoprothrombin C cofactor in a prothrombin activation mixture. Magnesium was not effective in either system. The role of different phospholipids in the complexing phenomenon was studied and compared with the suitability of the same phospholipids as prothrombin-activating cofactors of autoprothrombin C. All phospholipid preparations studied complexed with autoprothrombin C to some degree, but the most efficient complexing agents were found to be asolectin and a commercial phosphatidyl ethanolamine preparation, both materials being among the ones which demonstrated the highest prothrombin conversion activity. Since thrombin was not complexed under the same conditions, autoprothrombin C could be isolated from commercial thrombin preparations also containing autoprothrombin C. (Author)
Document Details
- Document Type
- Technical Report
- Publication Date
- Jun 29, 1964
- Accession Number
- AD0616934
Entities
People
- Edmond R. Cole
- J. L. Koppel
- John H. Olwin