Fibrinogen Degradation by Two Neutral Granulocyte Proteinases. Influence of Calcium on the Generation of Fibrinogen Degradation Products with Anticlotting Properties

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Abstract
Degradation of human fibrinogen by elastase-like proteinase, chymotrypsin-like proteinase and plasmin was done in the presence and absence of Ca ions, respectively. The resulting fibrinogen degradation products were tested for their coagulant and anti-coagulant properties. Fibrinogenolysis is delayed in the presence of Ca ions. Higher enzyme concentrations are required to get unclottable split products when Ca ions are present. The fibrinogen fragments obtained in the presence of Ca are different in their MW and anticoagulant activities compared to those obtained in the absence of Ca ions. This effect of Ca is most striking during fibrinogen cleavage by chymotrypsin-like proteinase. Elastase and plasmin-induced fibrinogenolysis was substantially influenced by Ca only at a late degradation stage.