Substrate Specificity of Tissue Type Plasminogen Activator

Human tissue-type plasminogen activator.

Tissue-type plasminogen activator (t-PA ) plays an important role in the removal of intravascular fibrin deposits and has several physiological roles and pathological activities in the brain. Its production by many other cell types suggests that t-PA has additional functions outside the vascular and central nervous system. Activity of t-PA is regulated at the level of its gene transcription, it...

Substrate specificity of tissue plasminogen activator and urokinase as determined with synthetic chromogenic substrates.

Three different synthetic chromogenic substrates )H-glutamylglycyl-L-arginine-p-nitroanilide (S-2227), pyro-glutamyl-glycyl-L-arginine-p-nitroanilide (S-2444), and H-D-isoleucyl-L-prolyl-L-arginine-p-nitroanilide (S-2288] were investigated for use in the measurement of plasminogen activator activity with high molecular weight urokinase (H-UK), low molecular weight urokinase (L-UK), and tissue p...

Deficiency Exacerbates Arthritis Tissue-Type Plasminogen Activator

Plasminogen and tissue-type plasminogen activator bind to immobilized fibronectin.

Fibronectin immobilized onto polystyrene surface was found to bind plasminogen and tissue-type plasminogen activator (t-PA) but only slightly the urokinase type as determined using mono- and polyclonal antibodies against the activators. Of the defined fibronectin fragments tested, the Mr 120,000-140,000 fragment was found to bind both plasminogen and t-PA. Proteolytically modified plasminogen (...

Optimizing refolding condition for recombinant tissue plasminogen activator

Low molecular size additives such as L-arginine and the redox compounds have been used both in the culturemedium and in vitro refolding to increase recombinant proteins production. Additives increase proteinrefolding and yield of active proteins by suppressing aggregate formation or enhancing refolding process.In this work, a comparative study was performed on refolding of rec...