Inactivation of trypsin-like proteases by sulfonylation. Variation of positively charged group and inhibitor length

Publisher Website
Google Scholar
Abstract
Attempts to achieve selective inactivation of serine proteases of closely related specificity (trypsin-like) by aryl sulfonylation were extended. Nitrophenyl esters of benzenesulfonic acid and phenylmethanesulfonic acid containing various positively charged groups were synthesized and examined as inactivation of trypsin, thrombin, plasmin, plasma kallikrein and urokinase. Examples of selective inactivation of isothiouronium derivatives were found and attributed to differences among these enzymes in geometry and flexibility of the primary specificity sites.