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- W1505772652 abstract "The p-nitrophenyl ester of p-amidinophenylmethanesulfonic acid had been found to inactivate thrombin by affinity labeling but did not have this action on other proteases of similar specificity such as trypsin, plasmin, or plasma kallikrein [Wong, S.-C., and Shaw, E., Arch. Biochem. Biophys. 161, 536 (1974)]. The ortho- and meta-nitrophenyl esters of this sulfonic acid have now been synthesized and shown to be less selective. In addition to thrombin, trypsin and plasma kallikrein are also inactivated. The ortho isomer is more effective than the meta. Plasmin is unaffected by all three esters. The results are interpreted to reflect geometrical differences in the first departing group subsite of these homologous active centers and to provide an additional structural basis for achieving selectivity of affinity labeling." @default.
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- W1505772652 date "1976-09-01" @default.
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- W1505772652 title "Inactivation of trypsin-like proteases by active-site-directed sulfonylation" @default.
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- W1505772652 doi "https://doi.org/10.1016/0003-9861(76)90146-6" @default.
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