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. 2015 Mar 31;6:95. doi: 10.3389/fphys.2015.00095

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Copyright © 2015 Kumar, Bhardwaj, Kumar and Mazumdar-Leighton.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Midgut trypsin and chymotrypsin activities detected using various synthetic substrates (A: BApNA; B: TAME; C: SAAPFAMC) in field-collected fourth instar P. brassicae larvae (n = 36) found feeding on cauliflower (CF-ctrl) and T. majus (TP-ctrl). Also shown are midgut serine protease activities in larvae transferred in the lab to detached mature leaves (ML), young leaves (YL) and curd/head (HD) of cauliflowers (CF) as well as leaves (L) and flowers (F) of T. majus. Specific activity refers to enzyme units hydrolyzed per minute per mg total protein. Bars depict mean ± SE; the same letters in lowercase are not statistically significant (p ≤ 0.05). Percent inhibition by STI of midgut trypsin and chymotrypsin activities detected in the midgut samples using (D) BApNA; (E) TAME; (F) SAAPFAMC substrates are shown. The extent of inhibition is shown relative to proteolytic activities detected in midgut samples (depicted as 100% in absence of STI).