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Trypsin complexed with α 1 ‐proteinase inhibitor has an increased structural flexibility
Author(s) -
Kaslik Gyula,
Patthy András,
Bálint Miklós,
Gráf László
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00816-r
Subject(s) - trypsin , proteolysis , biochemistry , serine , chemistry , enzyme , serpin , proteinase 3 , peptide sequence , amino acid , peptide , peptide bond , microbiology and biotechnology , biology , myeloperoxidase , immunology , inflammation , gene
Mutant rat trypsin Asp 189 Ser was prepared and complexed with highly purified human α 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 α 1 ‐proteinase inhibitor showed a highly increased susceptibility to enzymatic digestion. The peptide bond selectively attacked by bovine trypsin was identified as the Arg 117 ‐Val 118 one of trypsin. The structural and mechanistic relevance of this observation to serine proteinase‐substrate and serine proteinase‐serpin reactions are discussed.