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- W2075348916 abstract "1. Factor XIII was purified approximately 1000-fold from human plasma. 2. A quantitative assay for transamidase activity is described and was used to follow the activation of Factor XIII. 3. Activation by thrombin (EC 3.4.4.13) was time-dependent, was inhibited by Na-p-toluenesulphonyl-l-arginine methyl ester, had a pH optimum at 8.0, and gave a value of 1.2·10−6 M for Km. 4. Unlike bovine Factor XIII, thrombin activation of the human material proceed in the absence of calcium. 5. Activation by thrombin may be the result of limited proteolysis somewhat analogous to that responsible for the fibrinogen to fibrin conversion; the ability of reptilase to activate Factor XIII supports this idea though another coagulant enzyme, Arvin, was ineffective." @default.
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- W2075348916 date "1970-11-01" @default.
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- W2075348916 title "Studies on the activation of purified human factor XIII" @default.
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- W2075348916 doi "https://doi.org/10.1016/0304-4165(70)90129-7" @default.
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