Analysis Note
ε-Aminocaproic acid free
Plasma from each donor has been tested and found negative for antibody to HIV-1/HIV-2, antibody to HCV and HbSAg.
Biochem/physiol Actions
Plasminogen is the inactive precursor of the protease plasmin. Plasminogen is activated by the action of either tissue plasminogen activator (tPA), which primarily activates the fibrinolytic (thrombolytic) activity of plasmin, or urokinase plasminogen activator (uPA), which is associated with extracellular matrix remodeling and cell migration. Plasmin cleaves fibrin/fibrinogen and blood coagulation factors V/Va and VIII/VIIIa. It activates matrix metalloproteinases by cleaving the inactive proenzymes. It is also involved in the activation of some growth factors, such as vascular endothelial growth factor (VEGF) and transforming growth factor β (TGF-β).
Reconstitution
Solutions should be stored in buffer containing 20 mM lysine at neutral pH. The protein should be as concentrated as possible. Frozen in aliquots at −20 °C, it should be stable for several weeks.
Unit Definition
One unit will produce a ΔA275 of 1.0 from α-casein in 20 min at pH 7.5 at 37 °C, when measuring perchloric acid soluble products in a volume of 5.0 mL. Activity determined after activation to plasmin with urokinase.
Physical form
Lyophilized powder containing NaCl, EDTA, lysine and Tris buffer
Physical properties
Native-intact human plasminogen is a 291 amino acid glyco-protein with as many as 24 disulfide bonds. Plasminogen contains a single N-linked sialylated biantennary glycan. The two O-glycans possess a Gal β-1-3GalNAc core which are α-2-3 sialylated at the terminal Gal. An additional disialylated form has a second sialic acid residue with an α-2-6 linkage to GalNAc. Mono- and disialylated forms occur at a molar ratio of 80:20 in human plasminogen.