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- W2094415300 abstract "The amino-acid sequences of the acid-resistant inhibitors released from horse and pig inter-alpha-trypsin inhibitor (ITI) by tryptic proteolysis were determined. They are composed of two covalently linked Kunitz-type domains. In both cases the reactive site of their C-terminal antitryptic domains is occupied by arginine as in the homologous human and bovine inhibitors. The reactive site of their N-terminal domain exhibits only a weak interaction with polymorphonuclear granulocytic elastase and is occupied by leucine as in the strong elastase inhibitor released from bovine ITI. The differences between inhibitory activities of the ITI-derived inhibitors from horse, pig, and cattle are discussed on the basis of sequence differences in position P'2." @default.
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- W2094415300 date "1985-01-01" @default.
- W2094415300 modified "2023-09-25" @default.
- W2094415300 title "Kunitz-Type Proteinase Inhibitors Derived by Limited Proteolysis of the Inter-α-Trypsin Inhibitor, X. The Amino-Acid Sequences of the Trypsin-Released Inhibitors from Horse and Pig Inter-α-Trypsin Inhibitors" @default.
- W2094415300 doi "https://doi.org/10.1515/bchm3.1985.366.1.473" @default.
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