Site-directed mutations in the third domain of Bacillus thuringiensis delta-endotoxin CryIAa affect its ability to increase the permeability of Bombyx mori midgut brush border membrane vesicles.
A series of mutant Bacillus thuringiensis CryIAa delta-endotoxin proteins was prepared by replacing the first, second, and last arginine residues of the conserved third-domain sequence, R-521 YRVRIR-527, with other amino acids. The stable mutant proteins were bioassayed against Bombyx mori larvae an...
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| Yayımlandı: | Appl Environ Microbiol |
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| Asıl Yazarlar: | , , |
| Materyal Türü: | Artigo |
| Dil: | Inglês |
| Baskı/Yayın Bilgisi: |
American Society for Microbiology (ASM)
1996
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| Konular: | |
| Online Erişim: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC167797/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8572707/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/aem.62.1.279-282.1996 |
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