作者: Roxanne M. Broadway
DOI: 10.1002/(SICI)1520-6327(1996)32:1<39::AID-ARCH3>3.0.CO;2-S
关键词: Proteolytic enzymes 、 Trypsin 、 Kunitz STI protease inhibitor 、 Helicoverpa zea 、 Trypsin inhibitor 、 Biochemistry 、 Pieris rapae 、 Biology 、 Midgut 、 Serine Proteinase Inhibitors
摘要: Plant serine proteinase inhibitors (Pls) have the potential to restrict growth and/or development of herbivorous insects. However, there are limitations efficacy these Pls. An insect's susceptibility a Pl is determined, at least in part, by relative proportion proteolytic enzyme activity midgut that suppressed inhibitor. Insects adapt dietary trypsin inhibitor their host plant secreting “inhibitor-resistant” trypsin(s). These enzyme(s) may be standard proteinase(s) secreted into (e.g., Pieris rapae), or enhanced following ingestion Helicoverpa zea). In addition, insects pre-adapted specific Pl(s), adaptation from same family. For example, rapae crucifer specialist resistant cabbage Pl, but also Kunitz soybean inhibitor, family as non-host plant. The ultimate value this pre-adaptation herbivory species insect will determined number different families plant(s) which has adapted, and distribution those among other plants. Thus, it possible presence limits insect(s). multiple inhibitors, matched complement enzymes midgut, required enhance resistance plants © 1996 Wiley-Liss, Inc.