| Autor: |
Bulushova NV; Scientific Research Institute for Genetics and Selection of Industrial Microorganisms, Moscow, Russia. nat86@yandex.ru, Zhuzhikov DP, Lyutikova LI, Kirillova NE, Zalunin IA, Chestukhina GG |
| Jazyk: |
angličtina |
| Zdroj: |
Biochemistry. Biokhimiia [Biochemistry (Mosc)] 2011 Feb; Vol. 76 (2), pp. 202-8. |
| DOI: |
10.1134/s0006297911020064 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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