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Biochemical analysis reveals distinct plasmin-inhibitor complexes in human post-mortem plasma, indicating complete conversion of plasminogen and neutralization of fibrinolytic activity.
Human fibrinolytic post-mortem plasma was studied by G 200 gel filtration (GF), and gel electrophoresis (GE). It contained 2 compounds with plasminogen (PG) + plasmin (P) antigenicity, but no PG. One was a complex between P and α2macro-globulin (α2M) with GF partition coefficient (Kd)=0, and with no evidence of dissociation by GF or GE. It had a BAEesterase activity about that of P in normal plasma, as estimated and calculated from the molar catalytic amount of P (0.48 kU/μmol). The other was eluted later (Kd=0.17) but earlier than PG (Kd=0.33) and migrated between α2 and PG by GE. It had no esterase activity. Both were inactive against casein and fibrin. P was not associated with α1antitrypsin and inter-α-inhibitor.
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S. Müllertz (1972) studied this question.
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