Trypsin complexed with α1‐proteinase inhibitor has an increased structural flexibility
- 21 August 1995
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 370 (3) , 179-183
- https://doi.org/10.1016/0014-5793(95)00816-r
Abstract
Mutant rat trypsin Asp189Ser was prepared and complexed with highly purified human α1-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 α1-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 discussedKeywords
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