Abstract
Pancreatic elastase-induced degradation of some plasma proteins was studied in an in vitro model. The digestion was correlated with the degree of saturation of the alpha 1-proteinase inhibitor (alpha 1PI) and also with varying amounts of secretory leucocyte proteinase inhibitor (SLPI). SLPI was found to inhibit pancreatic elastase showing a Ki of about 10(-7) M for the complex. On the addition of human pancreatic elastase to plasma cleavage of C3, kininogen, fibrinogen and fibronectin was observed when the alpha 1PI approached saturation. In the present in vitro model it was possible to block the cleavage of the four plasma proteins, mentioned above completely with SLPI. Addition of the inhibitor also decreased the consumption of alpha 1PI.
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