Human and animal sera contain a globulin, plasminogen, which in the presence of activators is rapidly converted to plasmin, a proteolytic enzyme active at neutral hydrogen ion concentrations. Activators specific for plasminogen include streptokinase and staphylokinase of bacterial origin, urokinase and plasma activator found in body fluids, and fibrinokinase derived from tissues. Trypsin, an ac...

Human and animal sera contain a globulin, plasminogen, which in the presence of activators is rapidly converted to plasmin, a proteolytic enzyme active at neutral hydrogen ion concentrations. Activators specific for plasminogen include streptokinase and staphylokinase of bacterial origin, urokinase and plasma activator found in body fluids, and fibrinokinase derived from tissues. Trypsin, an ac...

Retinoic acid receptors (RARs) and retinoid X (RXRs) form heterodimers that activate target gene transcription by recruiting co-activator complexes in response to ligand binding. The nuclear receptor (NR) TIF2 mediates this recruitment interacting with the ligand-binding domain (LBD) of NRs trough interaction (TIF2NRID) containing three highly conserved ?-helical LxxLL motifs (NR-boxes). precis...

The binding of tissue-type plasminogen activator (t-PA) to fibrin is mediated both by its finger domain and by its kringle-2 domain. In this report, we investigate the relative affinities of these domains for lysine. Human recombinant t-PA deletion-mutant proteins were prepared and their ability to bind to lysine-Sepharose was investigated. Mutants containing the kringle-2 domain bound to lysin...