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Mutant rat trypsin AsplS9Ser was prepared and complexed with highly purified human al-proteinase inhibitor. The complex formed was purified to homogeneity and studied by N-terminal amino acid sequence analysis and limited proteolysis with bovine trypsin. As compared to uncomplexed mutant trypsin, the mutant enzyme complexed with oq-proteinase inhibitor showed a highly increased susceptibility to enzymatic digestion. The peptide bond selectively attacked by bovine trypsin was identiffed as the ArgnT-Va111s one of trypsin. The structural and mechanistic relevance of this observation to serine proteinasesubstrate and serine proteinase-serpin reactions are discussed.

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