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Isolation of a chitin‐binding lectin, with insecticidal activity in chemically‐defined synthetic diets, from two wild brassica species with resistance to cabbage aphid Brevicoryne brassicae
Author(s) -
Cole R. A.
Publication year - 1994
Publication title -
entomologia experimentalis et applicata
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.765
H-Index - 83
eISSN - 1570-7458
pISSN - 0013-8703
DOI - 10.1111/j.1570-7458.1994.tb01816.x
Subject(s) - biology , lectin , brevicoryne brassicae , chitin , biochemistry , brassica , agglutinin , aphid , wheat germ agglutinin , botany , glycine , pieris brassicae , amino acid , aphididae , homoptera , pest analysis , lepidoptera genitalia , chitosan
A lectin, with a chitin‐binding domain and chitinase activity, is present in significant quantities in the wild brassica species B. fruticulosa and B. spinescens but at low levels in cultivated cabbage cv. Offenham Compacta. The lectin, purified > 1000 fold after binding to chitin, migrated on SDS ‐ PAGE gels as a single band with a M r of 14.500. The amino acid composition of the lectin from B. spinescens indicated high concentrations of asparagine/aspartic acid, glycine, leucine and serine in common with other chitin‐binding lectins with insecticidal and antifungal activities. Brassica lectin and the closely related agglutinin from wheatgerm and nettle show significant insecticidal activity when presented to Brevicoryne brassicae in chemically‐defined synthetic diets.