The influence of various combinations of plasminogen and streptokinase on fibrinolysis. II. A mechanistic study.
The components found in 125I-labelled cross-linked plasma fibrin lysates obtained by alternate treatments with streptokinase (SK) and plasminogen (plgn) were examined by immunological and physicochemical methods. The more rapid and complete lysis achieved with the sequence SK leads to plgn was reflected by the near absence of the electrophoretically stable D dimer-E complex and high molecular weight soluble aggregates (greater than 3 x 10(5) molecular weight), while these components were present in considerable amounts during the plgn leads to SK regimen. An assessment of the data from the rapid and slow regimens suggested that cross-linked high molecular weight complexes wer initially released from fibrin, these being rapidly degraded to the D dimer-E complex which was subsequently converted to pure D dimer and E fragments. Two forms of the D dimer-E complex are proposed, probably varying in stability according to the number of attachment sites between the D dimer and E domains.
D004338:Drug Combinations; D004591:Electrophoresis, Polyacrylamide Gel; D005338:Fibrin Fibrinogen Degradation Products / Q000032:analysis*; D005342:Fibrinolysis; D006801:Humans; D007123:Immunoelectrophoresis, Two-Dimensional; D066298:In Vitro Techniques; D007457:Iodine Radioisotopes; D010958:Plasminogen / Q000494:pharmacology*; D013300:Streptokinase / Q000494:pharmacology*
D004338:Drug Combinations; D005338:Fibrin Fibrinogen Degradation Products; D007457:Iodine Radioisotopes; C015214:fibrinogen D fragment; C018543:fibrinogen fragment E; D010958:Plasminogen; D013300:Streptokinase