2Faculty of Biology, Lomonosov Moscow State University, 119991 Moscow, Russia; fax: (495) 939-4309
* To whom correspondence should be addressed.
Received September 22, 2010; Revision received October 19, 2010
A 67-kDa protein that can specifically bind the activated Cry9A endotoxin under ligand-blotting conditions was purified from midgut epithelium apical membranes of wax moth Galleria mellonella by affinity chromatography. N-Terminal amino acid sequencing enabled identification of this protein as aminopeptidase N. In similar experiments, 66- and 58-kDa proteins specific to endotoxin Cry3A were isolated from the midgut epithelium apical membranes of Tenebrio molitor larvae. Mass spectrometry showed close similarity of the 58-kDa protein to the Tenebrio molitor α-amylase.
KEY WORDS: δ-endotoxin, Bacillus thuringiensis, Galleria mellonella, Tenebrio molitor, toxin-binding protein