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dc.contributor.authorTheeraporn Puntheeranuraken_US
dc.contributor.authorSomphob Leetacheewaen_US
dc.contributor.authorGerd Katzenmeieren_US
dc.contributor.authorChartchai Krittanaien_US
dc.contributor.authorSakol Panyimen_US
dc.contributor.authorChanan Angsuthanasombaten_US
dc.contributor.otherMahidol Universityen_US
dc.date.accessioned2018-09-07T09:37:56Z-
dc.date.available2018-09-07T09:37:56Z-
dc.date.issued2001-07-31en_US
dc.identifier.citationJournal of Biochemistry and Molecular Biology. Vol.34, No.4 (2001), 293-298en_US
dc.identifier.issn12258687en_US
dc.identifier.other2-s2.0-0035630399en_US
dc.identifier.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0035630399&origin=inwarden_US
dc.identifier.urihttp://repository.li.mahidol.ac.th/dspace/handle/123456789/26456-
dc.description.abstractTryptic 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 this study, we constructed the recombinant clone over-expressing this putative pore-forming (PPF) fragment as inclusion bodies in Escherichia coli. The partially purified inclusions were composed of a 23-kDa protein, which cross-reacted with Cry4B antibodies, and whose N-terminus was identical to that of the 130-kDa protein. Dissimilar to protoxin inclusions, the PPF inclusions were only soluble when the carbonate buffer, pH 9.0, was supplemented with 6 M urea. After renaturation via a stepwise dialysis, the refolded PPF protein appeared to exist as an oligomer and was structurally stable upon trypsin treatment. Unlike the 130-kDa protoxin, the refolded protein was able to release entrapped glucose from liposomes, and showed comparable activity to the full-length activated toxin, although it lacks larvicidal activity. These results, therefore, support the notion that the PPF fragment that consists of α1-α5 of the activated Cry4B toxin is involved in membrane pore-formation.en_US
dc.rightsMahidol Universityen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0035630399&origin=inwarden_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.titleExpression and Biochemical Characterization of the Bacillus thuringiensis Cry4B α1-α5 Pore-forming Fragmenten_US
dc.typeArticleen_US
dc.rights.holderSCOPUSen_US
Appears in Collections:Scopus 2001-2005

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