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Flexibility and strictness in functional replacement of domain III of cry insecticidal proteins from Bacillus thuringiensis

Paper ID Volume ID Publish Year Pages File Format Full-Text
22287 43265 2007 3 PDF Available
Title
Flexibility and strictness in functional replacement of domain III of cry insecticidal proteins from Bacillus thuringiensis
Abstract

Cry1C, one of the lepidopteran-specific insecticidal proteins from Bacillus thuringiensis, exhibits potent cytotoxicity against Sf9, an insect cell line. Cry1Aa and Cry4A, which are lepidopteran- and dipteran-specific insecticidal proteins, respectively, show no cytotoxicity against Sf9. When domain III of Cry1C was replaced with that of Cry1Aa or Cry4A, the hybrid Cry1C protein retained the cytotoxicity. These results suggest that domain III of Cry1C is not crucial in determining the cytocidal specificity of Cry1C against Sf9.

Keywords
Bacillus thuringiensis; Sf9; cytotoxicity; Cry protein; domain exchangeGST, glutathione-S-transferase; LDH, lactate dehydrogenase
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Flexibility and strictness in functional replacement of domain III of cry insecticidal proteins from Bacillus thuringiensis
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 103, Issue 4, April 2007, Pages 381–383
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us