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Popykina N. A., Gladysheva I. P., Balabushevich N. G., Zamolodchikova T. S., Larionova N. I.
Interaction of Duodenase with Inhibitors of Microbic Origin
Abstract
Interaction of duodenase, proteinase with both trypsin- and
chymotrypsin-like substrate specificity, with chymostatin and leupeptin was
investigated. Ki of inhibition of duodenase hydrolysis of
Suc-Ala-Ala-Phe-pNA and N-t-Boc-O-Bz-Ser-Gly-Arg-pNA by chymostatin, was found
to be 63±4 nM. Mechanism of
inhibiton was found to be competitive, when Suc-Ala-Ala-Phe-pNA was used.
However when the N-t-Boc-O-Bz-Ser-Gly-Arg-pNA was used, mechanism of inhibition
was found to be uncompetitive. During studies on inhibition of duodenase by
isopropyonyl-leupeptin, 50% of enzyme activity was achieved when [I]0/[E]0
was 2000.
Copyright (C) Chemistry Dept., Moscow State University, 2002
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