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  • Title: Toxin-binding proteins isolated from yellow mealworm Tenebrio molitor and wax moth Galleria mellonella.
    Author: Bulushova NV, Zhuzhikov DP, Lyutikova LI, Kirillova NE, Zalunin IA, Chestukhina GG.
    Journal: Biochemistry (Mosc); 2011 Feb; 76(2):202-8. PubMed ID: 21568853.
    Abstract:
    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.
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