Lecadet, M.M. and Dedonder, R. (1967) Enzymatic hydrolysis of the crystals of Bacillus thuringiensis by the proteases of Pieris brassicae I. Preparation and fractionation of the lysates. Journal of Invertebrate Pathology, 9 (3). pp. 310-321.
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Abstract
The parasporal inclusion of Bacillus thuringiensis which resists the action of most proteases (trypsin, chymotrypsin, papain), is solubilized without previous denaturation by the proteases of Pieris brassicae. After completion of the hydrolysis a mixture of proteins, peptides, and free amino acids is obtained which can be separated on Sephadex G-75. The proteinaceous fraction consists of at least six components. The fractionation of the peptidic part by chromatography on Sephadex G-25 and DEAE Sephadex A-25 leads to the separation of four peptides with a molecular weight of the order of 5,000. The identification of the carboxylic end groups of these peptides and of the free amino acids shows that the nature of the peptide linkages which are hydrolyzed agrees with the specificity already determined for the proteases
| Item Type: | Article |
|---|---|
| Author Affiliation: | Service des Polyosides, Institut Pasteur, Paris, France |
| Subjects: | Crop Improvement |
| Divisions: | Other Crops |
| Depositing User: | Ms K Syamalamba |
| Date Deposited: | 02 May 2012 07:55 |
| Last Modified: | 02 May 2012 07:55 |
| Official URL: | http://dx.doi.org/10.1016/0022-2011(67)90065-1 |
| URI: | http://eprints.icrisat.ac.in/id/eprint/5039 |
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