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- W2070460219 abstract "A protease from the venom of the Southern Copperhead snake (Agkistrodon contortrix contortrix) that activates protein C was purified to homogeneity by a combination of sulfopropyl (SP)-Sephadex C-50, Sephadex G-150 and Mono-S column chromatography. The purified enzyme is a glycoprotein, and migrated as a single band in sodium dodecylsulfate-polyacrylamide gel electrophoresis with an apparent molecular weight of 37,000 under non-reducing conditions. Upon reduction with 2-mercaptoethanol, the enzyme exhibited a Mr of 40,000. The purified enzyme prolonged the clotting time of human plasma in a dose- and temperature-dependent manner. Purified bovine protein C was completely activated within 10 minutes upon incubation with the purified protease at a 1:500 enzyme: substrate ratio. This reaction was markedly inhibited by calcium ions. The purified venom protein C activator had no effect on human fibrinogen." @default.
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- W2070460219 date "1987-03-01" @default.
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- W2070460219 title "Isolation of a protein C activator from Southern Copperhead venom" @default.
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- W2070460219 doi "https://doi.org/10.1016/0006-291x(87)90337-8" @default.
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