Binding of tissue-type plasminogen activator with human endothelial cell monolayers. Characterization of the high affinity interaction with plasminogen activator inhibitor-1.

Abstract excerpt

The formation and release of covalent complexes between tissue-type plasminogen activator (t-PA) and plasminogen activator inhibitor-1 (PAI-1) limits the application of equilibrium radioligand binding analysis to characterize the interaction between t-PA and human umbilical vein endothelial cell (HUVEC) monolayers. To avoid this difficulty, we used a recombinant mutant of t-PA, S478A rt-PA, in which alanine has...

Topics

• Alanine
• Binding Sites
• Binding, Competitive
• Cells, Cultured
• Endothelium, Vascular
• Humans
• Kinetics
• Mutation
• Plasminogen Inactivators
• Recombinant Proteins