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domains via lysine residues allowing for the inhibition of plasmin. Another method of plasmin inactivation involves the cleavage of an ?2-macroglobulin at the bait region (a segment of the aM that is particularly susceptible to proteolytic cleavage) by plasmin. This initiates a conformational change such that the ?2-macroglobulin collapses about the plasmin. In the resulting ?2-macroglobulin-plasmin complex, the active site of plasmin is sterically shielded, thus substantially decreasing the plasmin's access

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