Fibrinogen degradation by two neutral granulocyte proteinases. Influence of calcium on the generation of fibrinogen degradation products with anticlotting properties.
Degradation of human fibrinogen by elastase-like proteinase, chymotrypsin-like proteinase and plasmin, was done in the presence and absence of calcium ions, respectively. The resulting fibrinogen degradation products were tested for their coagulant and anti-coagulant properties. The results show that 1. fibrinogenolysis is delayed in the presence of calcium ions. Higher enzyme concentrations are required to get unclottable split products when calcium ions are present. 2. The fibrinogen fragments obtained in the presence of calcium are different in their molecular weights and anticoagulant activities compared to those obtained in the absence of calcium ions. This effect of calcium is most striking during fibrinogen cleavage by chymotrypsin-like proteinase. Elastase and plasmin-induced fibrinogenolysis was substantially influenced by calcium only at a late degradation stage.
D001777:Blood Coagulation; D002118:Calcium / Q000494:pharmacology*; D002918:Chymotrypsin / Q000097:blood; D005340:Fibrinogen / Q000502:physiology*; D005341:Fibrinolysin / Q000378:metabolism; D006098:Granulocytes / Q000201:enzymology*; D006801:Humans; D007700:Kinetics; D008970:Molecular Weight; D010196:Pancreatic Elastase / Q000097:blood; D010446:Peptide Fragments / Q000032:analysis; D010447:Peptide Hydrolases / Q000097:blood*
D010446:Peptide Fragments; D005340:Fibrinogen; D010447:Peptide Hydrolases; D002918:Chymotrypsin; D010196:Pancreatic Elastase; D005341:Fibrinolysin; D002118:Calcium