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• W1518736614 abstract "In order to identify physiological activators of proteinase‐activated receptor‐2 (PAR‐2), a peptide chloromethane inhibitor (biotinyl‐Ser‐Lys‐Gly‐Arg‐CH 2 Cl) based on the cleavage site for activation of PAR‐2 was synthesised and tested with 12 trypsin‐like serine proteinases. The second‐order rate constant ( k i / K i ) for the formation of the covalent proteinase‐inhibitor complex varied by 2×10 5 ‐fold between the proteinases. Biotinyl‐Ser‐Lys‐Gly‐Arg‐CH 2 Cl reacted very rapidly with trypsin, acrosin from sperm and tryptase from mast cells: the k i / K i values with these proteinases were greater than 10 5 M −1 s −1 . Thus, the specificity of these proteinases matched the sequence of the activation site of PAR‐2 and it can be concluded that these proteinases are potential physiological activators of PAR‐2." @default.
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• W1518736614 date "1997-11-17" @default.
• W1518736614 modified "2023-10-14" @default.
• W1518736614 title "Identification of potential activators of proteinase‐activated receptor‐2¹" @default.
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• W1518736614 doi "https://doi.org/10.1016/s0014-5793(97)01298-2" @default.
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