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- W1547748619 endingPage "243" @default.
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- W1547748619 abstract "The following peptides were synthesized by classical methods in solution: Ac-Gly-Gly- Val-Arg-Gly-Pro-Arg-Val-Val-Glu-Arg-NHCH3 (A), Ac-Ala-Glu-Gly-Gly-Gly-Val- Arg-Gly-Pro-Arg-Val-Val-Glu-Arg-NHCH3 (B), and Ac-Phe-Leu-Ala-Glu-Gly-Gly- Gly-Val-Arg-Gly-Pro-Arg-Val-Val-Glu-Arg-NHCH3 (C). The rates of hydrolysis of the Arg-Gly bond of these three peptides by thrombin were measured, and the values of kcatKm were found to be 0.05 × 10−7 (A), 0.02 × 10−7 (B), and 1.6 × 10−7 (C) [(NIH units/ liter)s]−1. The value ofkcatKm for peptide C is less than 1% of that for fibrinogen [although the value of kcat itself, for peptide C (but not for A or B), is comparable to that for fibrinogen]. These results indicate that phenylanine and leucine at positions P9 and P8, respectively, play a key role in the reaction of thrombin with fibrinogen. The data also show that factors outside of the 16 residues of peptide C are important in determining the rate of hydrolysis of fibrogen by thrombin." @default.
- W1547748619 created "2016-06-24" @default.
- W1547748619 creator A5047719714 @default.
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- W1547748619 date "1977-07-01" @default.
- W1547748619 modified "2023-09-27" @default.
- W1547748619 title "Mechanism of action of thrombin on fibrinogen" @default.
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- W1547748619 doi "https://doi.org/10.1016/0003-9861(77)90303-4" @default.
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