K. Okada et al., EFFECTS OF ALPHA(2)-PLASMIN INHIBITOR ON PLASMINOGEN ACTIVATION BY STAPHYLOKINASE PLASMINOGEN COMPLEX, Thrombosis research, 76(2), 1994, pp. 211-220
Using a stable cross-linked SAK/plg complex, the effects of alpha(2)-p
lasmin inhibitor on plasminogen activation by SAK were investigated. a
lpha(2)-Plasmin inhibitor inhibited dose-dependently plasminogen activ
ation by the SAK/plg complex. When FCB-2 or EACA was added to the reac
tion mixture of SAK/plg complex and alpha(2)-plasmin inhibitor, the in
hibitory activity of alpha(2)-plasmin inhibitor was abolished and the
enzymatic activity of the complexes was restored. alpha(2)-Plasmin inh
ibitor inhibited the activity of the SK/plg complex, but neither FCB-2
nor EACA restored the plasminogen activator activity in the mixture o
f SK/plg complex and alpha(2)-plasmin inhibitor. Using I-125-labeled S
AK/plg complex with alpha(2)-plasmin inhibitor was analyzed. The SAK/p
lg complex produced a new complex with alpha(2)-plasmin inhibitor. The
formation of a new high molecular weight complex with alpha(2)-plasmi
n inhibitor was abolished by both EACA or FCB-2. With regard to the SK
/plg complex, neither EACA nor FCB-2 suppressed the complex formation
with alpha(2)-plasmin inhibitor. These findings indicate that the SAK/
plg complex binds to fibrin, that this complex expresses plasminogen a
ctivator activity without being affected by alpha(2)-plasmin inhibitor
.