Expression and Biochemical Characterization of the Bacillus thuringiensis Cry4B α1-α5 Pore-forming Fragment

Tryptic activation of the 130-kDa Bacillus thuringiensis Cry4B δ-endotoxin produced protease-resistant products of ca. 47 kDa and ca. 21 kDa. The 21-kDa fragment was identified as the N-terminal five-helix bundle (α1-α5), which is a potential candidate for membrane insertion and pore formation. In t...

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Bibliographic Details
Main Authors: Theeraporn Puntheeranurak, Somphob Leetacheewa, Gerd Katzenmeier, Chartchai Krittanai, Sakol Panyim, Chanan Angsuthanasombat
Other Authors: Mahidol University
Format: Article
Published: 2018
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Online Access:https://repository.li.mahidol.ac.th/handle/123456789/26456
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Institution: Mahidol University