Ontology type: schema:Chapter
1999
AUTHORSFredy Altpeter , Isabel Diaz , Heather McAuslane , Kamel Gaddour , Pilar Carbonero , Indra K. Vasil
ABSTRACTProteinase inhibitors have been proposed to be involved in the defence response against herbivorous pests (Hoffmann et al. 1992). The efficacy of a specific inhibitor depends on the structural compatibility of its reactive site with the substrate-binding site of the targeted proteinase. For example, trypsin-inhibitors include either an arginyl or lysyl residue, which is recognized by trypsin-like enzymes. Barley trypsin inhibitor CMe (BTI-CMe), an abundant protein in barley endosperm, is one of the best characterized members of the cereal multigene family of trypsin/α-amylase inhibitors (Carbonero and Gracia-Olmedo, 1998) and was first purified from barley flour as a protein of 14 KDa that was specifically active in vitro against trypsin. Recently BTI-CMe was shown to inhibit specifically the trypsin-like proteases of the gut extracts of the fall armyworm, Spodoptera frugiperda (Lepidoptera: Noctuidae) (Alfonso et al. 1997), whereas the BTI-CMe inhibitor is rapidly degraded in the digestive tract of mammals (unpublished data, Carbonero et al.). More... »
PAGES453-456
Plant Biotechnology and In Vitro Biology in the 21st Century
ISBN
978-94-010-5966-4
978-94-011-4661-6
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