Novel Preparation and Characterization of the α4-loop-α5 Membrane-perturbing Peptide from the Bacillus thuringiensis Cry4Ba δ-endotoxin
2006
Leetachewa, Somphob (Mahidol University, Salaya Campus, Nakornpathom, Thailand) | Katzenmeier, Gerd (Mahidol University, Salaya Campus, Nakornpathom, Thailand) | Anguthanasombat, Chanan (Mahidol University, Salaya Campus, Nakornpathom, Thailand), E-mail: stcas@mahidol.ac.th
Helices 4 and 5 of the Bacillus thuringiensis Cry4Ba δ-endotoxin have been shown to be important determinants for mosquito-larvicidal activity, likely being involved in membrane-pore formation. In this study, the Cry4Ba mutant protein containing an additional engineered tryptic cleavage site was used to produce the α4-α5 hairpin peptide by an efficient alternative strategy. Upon solubilization of toxin inclusions expressed in Escherichia coli and subsequent digestion with trypsin, the 130-kDa mutant protoxin was processed to protease-resistant fragments of ca. 47, 10 and 7 kDa.
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