Toxin-binding proteins isolated from yellow mealworm <Emphasis Type="Italic">Tenebrio molitor</Emphasis> and wax moth <Emphasis Type="Italic">Galleria mellonella</Emphasis> |
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Authors: | N V Bulushova D P Zhuzhikov L I Lyutikova N E Kirillova I A Zalunin G G Chestukhina |
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Institution: | Scientific Research Institute for Genetics and Selection of Industrial Microorganisms, Moscow, Russia. nat86@yandex.ru |
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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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