Diffusional transport of urokinase and acyl-urokinase into fibrin and plasma clots: time of contact and fibrinolytic response in vitro
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Summary
The effect of short-time contacts of fibrin and plasma clots with solutions of urokinase and acyl-urokinase in a buffer or human blood plasma on the degree and duration of fibinolysis was studied in vitro.
- Type
- article
- Published
- 2001-10-01
- Cited by
- 0
- References
- 19
- OpenAlex
- https://openalex.org/W6922467
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:81689789
Keywords
Urokinase, Chemistry, Fibrinolysis, Fibrin, Lysis
References
- Activation of fibrin-bound plasminogen by pro-urokinase and its complementariness with that by tissue plasminogen activator.
- Cross-linking of alpha 2-plasmin inhibitor to fibrin by fibrin-stabilizing factor.
- Dependence of Blood Clot Lysis on the Mode of Transport of Urokinase into the Clot - A Magnetic Resonance Imaging Study in Vitro
- Rearrangements of the Fibrin Network and Spatial Distribution of Fibrinolytic Components during Plasma Clot Lysis
- Tissue plasminogen activator and urokinase mediate the binding of Glu-plasminogen to plasma fibrin I. Evidence for new binding sites in plasmin-degraded fibrin I.
- The effects of fibrinogen and its cleavage products on the kinetics of plasminogen activation by urokinase and subsequent plasmin activity.
- The binding of human plasminogen to fibrin and fibrinogen.
- Kinetics of the activation of plasminogen by human tissue plasminogen activator. Role of fibrin.
- Interaction between plasminogen activator inhibitor type 1 (PAI-1) bound to fibrin and either tissue-type plasminogen activator (t-PA) or urokinase-type plasminogen activator (u-PA). Binding of t-PA/PAI-1 complexes to fibrin mediated by both the finger and the kringle-2 domain of t-PA.
- Prolonged plasma clot lysis induced by acyl-derivatives of urokinase in vitro
- Tissue-type plasminogen activator increases the binding of glu-plasminogen to clots.
- Differences in the binding to fibrin of native plasminogen and plasminogen modified by proteolytic degradation. Influence of omega-aminocarboxylic acids.
- Principles of Biochemistry
- Inner clot diffusion and permeation during fibrinolysis.
- High-affinity binding sites for human Glu-plasminogen unveiled by limited plasmic degradation of human fibrin.
- Initial plasmin-degradation of fibrin as the basis of a positive feed-back mechanism in fibrinolysis.
- Binding of plasminogen activators to fibrin: characterization and pharmacological consequences.
- The Influence of Transport Parameters and Enzyme Kinetics of the Fibrinolytic System on Thrombolysis: Mathematical Modelling of Two Idealised Cases
- Fibrinolytic agents
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