EGFP as a fusion partner for the expression and organic extraction of small polypeptides
| Autor: | Lubov I Popova, Leonid M. Vinokurov, Vitaly S. Skosyrev, Vasily E. Zagranichny, Mikhail V Zakharov, Andrey Yu. Gorokhovatsky, Natalja V Rudenko, Alexander V. Yakhnin |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
Recombinant Fusion Proteins
Green Fluorescent Proteins Molecular Sequence Data Gene Expression medicine.disease_cause Peptides Cyclic Green fluorescent protein 3' 5'-Cyclic-GMP Phosphodiesterases Escherichia coli Fatty Acid Synthase Type II medicine Fluorescent protein Cyclic Nucleotide Phosphodiesterases Type 6 Fusion Base Sequence biology fungi Extraction (chemistry) biology.organism_classification Fusion protein DNA-Binding Proteins Luminescent Proteins Biochemistry Insect Proteins Carrier Proteins Peptides Bacteria Intracellular Acetyl-CoA Carboxylase Antimicrobial Cationic Peptides Biotechnology |
| Zdroj: | Protein Expression and Purification. 27:55-62 |
| ISSN: | 1046-5928 |
| DOI: | 10.1016/s1046-5928(02)00595-8 |
| Popis: | Green fluorescent protein (GFP) is widely used as an excellent reporter module of the fusion proteins. The unique structure of GFP allows isolation of the active fluorescent protein directly from the crude cellular sources by extraction with organic solvents. We demonstrated the stable expression of four short polypeptides fused to GFP in Escherichia coli cells, including antimicrobial cationic peptides, which normally kill bacteria. EGFP module protected fusion partners from the intracellular degradation and allowed the purification of the chimerical proteins by organic extraction. The nature of the polypeptide fused to GFP, as opposed to the order of GFP and the polypeptide modules in the fusion protein, influenced the efficiency of the described purification technique. |
| Databáze: | OpenAIRE |
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