Carp Fibrinogen and Its Terminal Plasmin Degradation Products
نویسندگان
چکیده
The isolation and characterization of carp (Cyprinus carpio) plasma fibrinogen and its plasmin degradation products are described. Alike other vertebrate species, carp fibrinogen is a dimeric protein and consists of three different pairs of disulfide-bonded polypeptide chains. Aa, B/f, and y. In contrast to mammalian fibrinogen, the B0 chain of carp fibrinogen has apparently a higher molecular weight than Aa chain. The relatively large size of the carp B/J chain results from the unusually large size of the NH2-terminal B fibrinopeptide released by thrombin cleavage of fibrinogen. As in mammalian species, plasmin digestion of carp fibrinogen produced as main terminal endproducts two classes of fragments D and E. It was found that fragment D (D,) inhibited fibrin monomer polymerization not only in homobut in heterologous system as well.
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