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- W4231558082 abstract "Purified thrombin-C loses its clotting power upon acetylation. The thrombin-E which is produced during the acetylation has approximately twice the proteolytic activity as the original thrombin-C. Evidently amino groups are not necessary to have thrombin-E activity, but if o-acyl groups are also produced the enzyme does not hydrolyze p-toluenesulphonylarginine methyl ester (TAMe). The activity can be recovered by spontaneous hydrolysis of the o-acyl groups at pH 8.5. Thrombin-E does not activate fibrinogen, but does lyse fibrin. The optimum pH with TAMe as substrate is 8.8. It may be that thrombin-C is a dimer of the basic structure in thrombin-E." @default.
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- W4231558082 date "1959-01-01" @default.
- W4231558082 modified "2023-10-16" @default.
- W4231558082 title "THE ACETYLATION OF THROMBIN" @default.
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- W4231558082 doi "https://doi.org/10.1139/y59-150" @default.
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