Human α-1-antichymotrypsin: interaction with chymotrypsin-like proteinases

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Abstract
The interaction of human plasma .alpha.-1-antichymotrypsin with serine proteinases from different tissues has been investigated. The protein formed stable complexes with pancreatic chymotrypsin, leukocyte cathepsin G and mast cell chymotrypsin. No inhibition of pancreatic trypsin of leukocyte elastase could be demonstrated. With mixtures containing both .alpha.-1-antichymotrypsin and .alpha.-1-proteinase inhibitor, the former preferentially inactivated leukocyte cathepsin G, while the latter showed a strong preference for pancreatic chymotrypsin. However, leukocyte elastase was specifically inactivated by .alpha.-1-proteinase inhibitor even in 1:1 mixtures with chymotrypsin. These results suggest that one of the primary functions of .alpha.-1-antichymotrypsin is to inactivate leukocyte cathepsin G, while .alpha.-1-proteinase inhibitor controls the activity of other serine proteinases, particularly leukocyte elastase.

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