| Autor: |
Yaoi, Katsuro, Kadotani, Tomoyuki, Kuwana, Hisanaga, Shinkawa, Ayaka, Takahashi, Tsuyoshi, Iwahana, Hidenori, Sato, Ryoichi |
| Předmět: |
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| Zdroj: |
European Journal of Biochemistry; 6/15/97, Vol. 246 Issue 3, p652-657, 6p |
| Abstrakt: |
Cry1Aa toxin-binding proteins from the midgut brush border membrane vesicles of Bombyx mori, a toxin-susceptible silkworm, were analyzed to find candidates for the toxin receptors. Ligand blotting showed that Cry1Aa toxin bound to a 120-kDa protein. A part of the 120-kDa protein was solubilized from the membrane vesicles with phosphatidylinositol-specific phospholipase C, resulting in a 110-kDa protein which therefore may be linked to a glycosyl-phosphatidylinositol anchor. The 120-kDa and 110- kDa Cry1Aa toxin-binding proteins were solubilized with detergent or pohosphatidylinositol-specific phospholipase C, respectively, and purified using anion-exchange chromatography. Scatchard plot analysis for the specific binding of purified 110-kDa protein to Cry 1Aa toxin yielded a Kd value of 7.6 nM, which was similar to that for the binding of intact brush border membrane vesicles to the toxin. N-terminal and internal amino acid sequences of the 120-kDa and 110-kDa proteins showed high degrees of similarity to those of aminopeptidase N, a putative Cry1 Ac toxin receptor, reported in Manduca sexta and Heliothis virescens. On this basis, the 120-kDa CryIAa toxin-binding protein from B. mori was identified as a member of the aminopeptidase family. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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