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The Receptor for Bacillus Thuringiensis Cry 1Ac Delta-endotoxin in the Brush Border Membrane of the Lepidopteran Helicoverpa armigera is Aminopeptidase N

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Author(s): Kausar Malik | Tariq Mahmood | S. Riazuddin

Journal: Journal of Biological Sciences
ISSN 1727-3048

Volume: 1;
Issue: 8;
Start page: 782;
Date: 2001;
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Keywords: Lepidopteran | helicoverpa armigera | Delta-endotoxin | amono-peptidase | alkaline-phosphate | Ligand-blotting | homology

ABSTRACT
120 Kda and 70 Kda protein in the larval midgut membrane of the lepidopteran Helicoverpa armigera identified as putative receptor for Bt Cry 1Ac delta-endotoxin .Receptor proteins have been purified by a combination of gel-filtration and anion exchange chromatography .In ligand-blotting experiment ,the purified protein has binding capacity with Cry 1Ac and Cry 1Ab but not to Cry 2A .N-terminal sequence obtained from the protein show no homology to already existing sequences .When assayed for amino-peptidase and alkaline phosphatase activities , purified receptors preparations were enriched 2.5 fold in amino-peptidase activity compare to Helicoverpa-armigera brush border membrane vesicles . The 70 Kda protein seems to be the part of 120 Kda receptor protein.
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