Lookup NU author(s): Professor Angharad MR Gatehouse,
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
Three distinct digestive protease activities, with strongly alkaline pH optima, were identified in the gut of tomato moth (Lacanobia oleracea) larvae, and characterised using specific synthetic substrates and inhibitors. These were; a trypsin-like activity, a chymotrypsin-like activity specific for substrates and inhibitors containing more than one amino acid residue, and an elastase-like activity, accounting for 40%, 30% and 20% of overall proteolysis respectively. The protease activities differed in their sensitivities to inhibition by different plant protein protease inhibitors (PIs), as estimated by I-50 values. Soya bean Kunitz trypsin inhibitor (SKTI) was the only plant PI tested to inhibit all three digestive protease activities at concentrations <40 mu g/ml (approx. 5x10(-6)M). Incorporation of SKTI into a potato leaf-based artificial diet at 2% of total protein, decreased larval survival and growth (by approx. 33% and 40% respectively after 21 days) and retarded development (by approx. 2 days). However, when SKTI was expressed in transgenic potato plants at approx. 0.5% of total protein, only marginal effects on L. oleracea larvae were observed, which decreased with time. Whilst the presence of SKTI in artificial diet increased endogenous larval trypsin-like activity by up to four-fold, no effects on this activity were observed in larvae feeding on transgenic plants. (C) 1999 Elsevier Science Ltd. All rights reserved.
Author(s): Davison GM; Gatehouse AMR; Norton E; Babbe SM; Newell CA; Gatehouse JA
Publication type: Article
Publication status: Published
Journal: Journal of Insect Physiology
Print publication date: 01/06/1999
ISSN (print): 0022-1910
ISSN (electronic): 1879-1611
Publisher: Elsevier Science Ltd.
Altmetrics provided by Altmetric