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FEBS Lett. 1995 Aug 21;370(3):179-83.

Trypsin complexed with alpha 1-proteinase inhibitor has an increased structural flexibility.

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  • 1Department of Biochemistry, Eötvös University, Budapest, Hungary.


Mutant rat trypsin Asp189Ser was prepared and complexed with highly purified human alpha 1-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 alpha 1-proteinase inhibitor showed a highly increased susceptibility to enzymatic digestion. The peptide bond selectively attacked by bovine trypsin was identified as the Arg117-Val118 one of trypsin. The structural and mechanistic relevance of this observation to serine proteinase-substrate and serine proteinase-serpin reactions are discussed.

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