Cloning and expression of rapeseed procruciferin in Escherichia coli and crystallization of the purified recombinant protein
| Autor: | Shigeru Utsumi, Mary Rose G. Tandang, Motoyasu Adachi |
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| Rok vydání: | 2004 |
| Předmět: |
clone (Java method)
Protein Conformation Molecular Sequence Data Sequence Homology Bioengineering Biology Protein Engineering medicine.disease_cause Applied Microbiology and Biotechnology law.invention Conserved sequence chemistry.chemical_compound law Escherichia coli medicine Amino Acid Sequence Cloning Molecular Cells Cultured Plant Proteins chemistry.chemical_classification Cloning Brassica rapa Seed Storage Proteins Gene Expression Regulation Bacterial General Medicine Protein engineering Allergens Antigens Plant Recombinant Proteins Amino acid chemistry Biochemistry Seeds Recombinant DNA Crystallization DNA Biotechnology |
| Zdroj: | Biotechnology Letters. 26:385-391 |
| ISSN: | 0141-5492 |
| Popis: | Two rapeseed cruciferin cDNAs (cru2/3a and cru2/3b) were cloned and sequenced. A comparison of their DNA and protein sequences with other cruciferins, indicated cru2/3b to be a novel clone and, among them, an inherent and highly conserved sequence of twelve amino acids was identified. Procruciferin 2/3a and 2/3b were expressed in Eschericha coli, and procruciferin 2/3a was obtained in a soluble form. The expressed procruciferin 2/3a has a trimeric structure and formed crystals although the quality was not good, suggesting that this expression system is useful for protein engineering of procruciferin 2/3a. |
| Databáze: | OpenAIRE |
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