Abstract
Ultracentrifugation and enzyme kinetic studies with casein (pH stat) and LME assays have demonstrated that the immediate plasma plasmin inhibitor is a high-density protein which acts as a noncompetitive inhibitor of plasmin. The affinity of this inhibitor for plasmin (1.7×107M) is about three to five magnitudes greater than the affinity of casein (9.0×104M) or LME (5.5×101M) for plasmin. This supports the concept that this inhibitor can act effectively under physiologic conditions to protect proteins which are susceptible to digestion by plasmin in vivo.
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