Related Experiment Videos

Identification of the plasminogen activator secreted by human fibroblasts

S A Cederholm-Williams, N W Porter

The British Journal of Dermatology

|April 1, 1984

Abstract:

Plasminogen activator was partially purified from cultured human fibroblasts. The enzyme binds to fibrin, has a molecular weight of 68,000 and is antigenically identical to human uterine tissue plasminogen activator.

Related Concept Videos

Articles linked to this work by shared authors, journal, and citation graph.

[Modifying effect of antiplasminogen monoclonal antibody IV-1c on human plasmin catalytic properties].

Ukrains'kyi biokhimichnyi zhurnal (1999 )·2004

[Role of lysine binding sites in activation of plasminogen by streptokinase].

Ukrains'kyi biokhimichnyi zhurnal (1999 )·2003

[Degradation of streptokinase and the catalytic properties of the plasmin-streptokinase complex].

Ukrains'kyi biokhimichnyi zhurnal (1999 )·2003

[Isolation and characteristics of antistreptokinase antibodies from blood serum of myocardial infarct patients treated with streptokinase].

Ukrains'kyi biokhimichnyi zhurnal (1999 )·2000

[Features of plasminogen activation in a complex with antiplasminogen monoclonal antibody IV-1C].

Ukrains'kyi biokhimichnyi zhurnal (1999 )·2000

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 peptide.

The Biochemical journal·1998

See all related articles