Tissue plasminogen activator connection

In a similar fashion, polyethylene glycol can be activated with CDI for connection to a protein, as has been shown for superoxide dismutase, a2-macroglobulin, a2-macro-globulin-trypsin, lactoferrin, and tissue plasminogen activator t208] [209]... 

The epidermal growth factor (EGF) domain is one example of a module that is present in several proteins (Figure 3-8). EGF is a small, soluble peptide hormone that binds to cells in the embryo and in skin and connective tissue in adults, causing them to divide. It is generated by proteolytic cleavage between repeated EGF domains in the EGF precursor protein, which is anchored in the cell membrane by a membrane-spanning domain. EGF modules are also present in other proteins and are liberated by proteolysis these proteins include tissue plasminogen activator (TPA), a protease that is used to dissolve blood clots In heart attack victims ... 

The carboxy-terminal region in apolipoprotein (a) closely resembles the protease domain in plasminogen [eight amino acid substitutions, nine amino acid deletions, and one insertion in apo(a) relative to plasminogen, with 94% overall nucleotide sequence identity] (G28). The most important difference is the substitution of arginine by serine in the site responsible for proteolytic activity (position 4308) (G28). As a result, Lp(a) has no protease activity towards substrates for plasmin (J3). Salonen (SI) reported a serine-protease activity of Lp(a) towards fibronectin, a glycoprotein present in connective tissue matrices. 

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