Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:3.4.21.7 (
plasmin
)
9,023
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
3-Hydroxypropyl flufenamide (Flu-
HPA
) is one of a series of flufenamic acid derivatives that enhances blood clot lysis in vitro. Studies of possible mechanisms of action of Flu-
HPA
were undertaken. The profibrinolytic activity of Flu-
HPA
in clot lysis assays was found to be dependent on plasminogen. The influence of Flu-
HPA
on the ability of purified alpha 2-antiplasmin to inhibit purified
plasmin
was studied. Plasmin activity was determined using 125I-fibrin plates or the spectrophotometric tripeptide substrate, Val-Leu-Lys-paranitroanilide. At Flu-
HPA
concentrations greater than 1 mM, the inhibitory activity of alpha 2-antiplasmin was abolished in a time-dependent and concentration-dependent manner. The influence of Flu-
HPA
on the ability of purified Cl inhibitor to inhibit purified plasma kallikrein and beta-Factor XIIa was also studied. Cl inhibitor activity was abolished by Flu-
HPA
at concentrations greater than 2 mM. Notably, Flu-
HPA
up to 60 mM did not affect the amidolytic activities of
plasmin
, kallikrein, or beta-Factor XIIa. Flu-
HPA
did not release enzyme activity from preformed complexes of either alpha 2-antiplasmin and
plasmin
of Cl inhibitor and kallikrein. A water-soluble derivative of flufenamic acid, N-flufenamyl-glutamic acid, also inactivated alpha 2-antiplasm and Cl inhibitor. This inactivation was shown to be reversible. These results indicate that synthetic fibrinolytic compounds such as flufenamic acid derivatives may promote fibrinolysis by directly inactivating alpha 2-antiplasmin and Cl inhibitor.
...
PMID:Inactivation of purified human alpha 2-antiplasmin and purified human C1 inhibitor by synthetic fibrinolytic agents. 645 20
HPA
of 85.5% purity was synthesized by the solid phase method on HPLC. The data obtained from amino acid analysis and fast atom bombardment were in good agreement with the theoretical values. The studies on the biological activity demonstrated the peptide inhibited efficiently the in vitro ADP-induced human platelet aggregation. In vivo, the peptide increased evidently the activity of
plasmin
and inhibited experimental thrombosis in the rabbit.
...
PMID:Studies on the synthesis and Antithrombosis Activity of the Analogue of Fibrin Decomposed Product-Related Peptide. 1223 97
