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• W1967331384 abstract "A peptide, which was released accompanying with the activation of bovine plasma fibrin stabilizing factor (FSF) by thrombin, was isolated and characterized. The peptide consisted of Asp4, Thr3, Ser4, Glu4, Pro5, Gly4, Ala4, Val2, Ile1, Leu2, Phe1, and Arg3. The content of proline was highest in all of these amino acids. The carboxyl-terminal residue of the peptide was identified as arginine. However, no N-terminal amino acid reactive with phenylisothiocyanate and dansyl chloride could be determined. Edman degradation on the inactive FSF showed glutamic acid or glutamine as one N-terminal residue. After the activation of FSF by thrombin, glycine was identified as a second N-terminal residue, in addition to glutamic acid (glutamine). These results indicate that the transformation of FSF to the active enzyme by thrombin involves proteolysis of an arginyl-glycyl bond located in the N-terminal region of one of the subunits of the proenzyme." @default.
• W1967331384 created "2016-06-24" @default.
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• W1967331384 date "1973-10-01" @default.
• W1967331384 modified "2023-10-12" @default.
• W1967331384 title "A peptide released from plasma fibrin stabilizing factor in the conversion to the active enzyme by thrombin" @default.
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• W1967331384 doi "https://doi.org/10.1016/0006-291x(73)91141-8" @default.
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