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- W1968793896 abstract "Abstract 1. 1. Kinetic parameters and specificity characteristics have been determined for N -( β -pyridylmethyl)-3,4-dichlorophenoxyacetamide- p -fluorosulfonylacetanilide bromide (PDFA), a member of a new class of active-site-directed irreversible protease inhibitors where covalent bonding to the enzymes occurs outside the limits of the active site proper. The results establish PDFA as one of the most potent inhibitors of α-chymotrypsin (EC 3.4.4.5) with a second-order rate constant of inactivation of 5.41 · 10 4 M −1 · min −1 at pH 7.0 and 37 °C. 2. 2. PDFA is also a weak irreversible inhibitor of trypsin (EC 3.4.4.4), pancreatic kallikrein (EC 3.4.4.21), elastase (EC 3.4.4.7) and thrombin (EC 3.4.4.13), in this approximate descending order of effectiveness. The second-order rate constant of inhibition with trypsin (at pH 8.1) is more than 200 times lower than with α-chymotrypsin (at pH 7.0)." @default.
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- W1968793896 date "1973-09-01" @default.
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- W1968793896 title "On the irreversible inhibition of α-chymotrypsin, trypsin, pancreatic kallikrein', thrombin and elastase by N-(β-pyridylmethyl)-3,4 dichlorophenoxyacetamide-p-fluorosulfonylacetanilide bromide" @default.
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- W1968793896 doi "https://doi.org/10.1016/0005-2744(73)90084-3" @default.
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