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Article

Tissue-type plasminogen activator and its substrate Glu-plasminogen share common binding sites in limited plasmin-digested fibrin.

The Journal of biological chemistry - 15 Aug 1990

de Vries C, Veerman H, Koornneef E, Pannekoek H

Abstract excerpt

The enzyme tissue-type plasminogen activator (t-PA) and its substrate Glu-plasminogen can both bind to fibrin. The assembly of these three components results in about a 1000-fold acceleration of the conversion of Glu-plasminogen into plasmin. Fibrin binding of t-PA is mediated both by its finger (F) domain and its kringle-2 domain. Fibrin binding of Glu-plasminogen involves its kringle structures (K1-K5). It has...

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PMID: 2143185

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Tissue-type plasminogen activator and its substrate Glu-plasminogen share common binding sites in limited plasmin-digested fibrin.PMID 2143185Read ↗

The role of the finger domain of tissue-type plasminogen activator (t-PA) and plasminogen activator inhibitor 1 (PAI-1) in initiation and progression of thrombolysis.Semantic proximity Read ↗

Kinetic characterization of tissue-type plasminogen activator (t-PA) and t-PA deletion mutants.Semantic proximity Read ↗

Kringle 1 domain of human tissue-type plasminogen activator is a functional module mediating fibrinogen-stimulated plasminogenolytic activity.Semantic proximity Read ↗

Evidence that the conformation of unliganded human plasminogen is maintained via an intramolecular interaction between the lysine-binding site of kringle 5 and the N-terminal peptideSemantic proximity Read ↗

PlasminogenSemantic proximity Read ↗

The kringle domains of human plasminogen.Semantic proximity Read ↗

Involvement of aspartic and glutamic residues in kringle-2 of tissue-type plasminogen activator in lysine binding, fibrin binding and stimulation of activity as revealed by chemical modification and oligonucleotide-directed mutagenesis.Semantic proximity Read ↗

Fibrin affinity and clearance of t-PA deletion and substitution analogues.Semantic proximity Read ↗

Biochemical and functional characterization of human tissue-type plasminogen activator variants obtained by deletion and/or duplication of structural/functional domains.Semantic proximity Read ↗

Rapid-reaction kinetic characterization of the pathway of streptokinase-plasmin catalytic complex formation.Semantic proximity Read ↗

Identification of the mechanism responsible for the increased fibrin specificity of TNK-tissue plasminogen activator relative to tissue plasminogen activator.Semantic proximity Read ↗

The plasminogen (fibrinolytic) system.Semantic proximity Read ↗

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