COMPARISON OF POLYMERIZATION OF ANCROD AND THROMBIN FIBRIN MONOMERS

  • 1 January 1977
    • journal article
    • research article
    • Vol. 50  (4) , 619-624
Abstract
The polymerization of thrombic [human] and ancrod [from Ancistrodon rhodostoma] fibrin monomers was studied with a standardized technique that evaluated turbidity changes and protein incorporation into the clot. Ancrod fibrin monomers polymerized more slowly and formed less turbid clots (at identical protein concentrations). Changes in ionic strength and pH influenced ancrod fibrin monomer polymerization to a greater extent than thrombin fibrin monomer polymerization. Benzyltriethylammonium chloride was a potent inhibitor of fibrin monomer polymerization, with a greater inhibitory effect on ancrod fibrin monomers than on thrombin fibrin monomers. The differences between ancrod and thrombin fibrin may play a role in the infrequent thrombotic complications reported with ancrod therapy.

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