| Autor: |
Chiara Lubelli, Fiorenzo Stirpe, Sijmie Heerkens, Louis Boon, Mark de Boer, Marcel T. den Hartog, Antonio P. Ortiz Buijsse |
| Rok vydání: |
2002 |
| Předmět: |
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| Zdroj: |
European Journal of Biochemistry. 269:1772-1779 |
| ISSN: |
0014-2956 |
| DOI: |
10.1046/j.1432-1327.2002.02823.x |
| Popis: |
Bouganin is a ribosome-inactivating protein that recently was isolated from Bougainvillea spectabilis Willd. In this work, the cloning and expression of the cDNA encoding for bouganin is described. From the cDNA, the amino-acid sequence was deduced, which correlated with the primary sequence data obtained by amino-acid sequencing on the native protein. Bouganin is synthesized as a pro-peptide consisting of 305 amino acids, the first 26 of which act as a leader signal while the 29 C-terminal amino acids are cleaved during processing of the molecule. The mature protein consists of 250 amino acids. Using the cDNA sequence encoding the mature protein of 250 amino acids, a recombinant protein was expressed, purified and characterized. The recombinant molecule had similar activity in a cell-free protein synthesis assay and had comparable toxicity on living cells as compared to the isolated native bouganin. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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