INHIBITION OF THROMBIN BY SARIN.
Abstract
Sarin was found to inhibit the clotting and esterase activities of bovine thrombin. When a crude source, topical thrombin was employed, clotting was more sensitive to inhibition than was esterase activity. Upon partial purification of the enzyme, ester hydrolysis and fibrinogen clotting became equally sensitive to inhibition by sarin. These differences can be ascribed to the removal of a contaminant enzyme, which would hydrolyze the ester and yet be less sensitive to the inhibitor. This explanation also accounts for discrepancies in the literature involving thrombin inhibition by diisopropyl fluorophosphate. Spontaneous reactivation of sarin-inhibited thrombin occurred slowly. With high concentrations of pralidoxime chloride, reactivation was more rapid, being complete within 24 hours. The inhibited thrombin did not lose its ability to be reactivated by the oxime after 24 hours. (Author)
Document Details
- Document Type
- Technical Report
- Publication Date
- Sep 01, 1969
- Accession Number
- AD0695618
Entities
People
- Arthur R. Thompson