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  • Title: [Anticlotting activity of fragment D from fibrinogen and fibrin and its dependence on calcium presence when fragments are obtained from fibrinogen].
    Author: Tolstikh VM, Varets'ka TV.
    Journal: Ukr Biokhim Zh; 1976; 48(1):116-21. PubMed ID: 1258156.
    Abstract:
    The CaCl2 concentration of about 10(-4) M slightly reduces the proteolytic fibrinogen degradation and greatly increases the anticlotting activity in the arising fragments D. With a rise in the CaCl2 concentration to 10(-2) M a subsequent limitation of proteolysis occurs, but less active fragments D are formed. These facts suggest that a moderate restriction of peptide bond cleavage enhances the fragment D activity, whereas excessive restriction exhibits an adverse effect. Fragment D originating from noncross-linked fibrin inhibits clotting stronger than its counterpart--the fibrinogen derivative. The following explanation seems plausible. Certain sites of the intact molecules, essential for the inhibitory activity of the prospective fragment D, become somewhat "enzyme-proof" (due to intermolecular links characteristic of polymeric fibrin), thus, avoiding proteolytic damage. Calcium ions presented at the optimum concentration may act similarly.
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