Leishmania mexicana amazonensis: Development of a peptide tag useful for labeling and purifying biotinylated recombinant proteins
| Autor: | Siegfried Detke |
|---|---|
| Rok vydání: | 2007 |
| Předmět: |
Carboxy-Lyases
Recombinant Fusion Proteins Blotting Western Leishmania mexicana Immunology law.invention Gene product chemistry.chemical_compound Transformation Genetic Biotin law Animals Biotinylation Carbon-Nitrogen Ligases Horseradish Peroxidase biology Escherichia coli Proteins General Medicine Avidin biology.organism_classification Fusion protein Molecular biology Repressor Proteins Klebsiella pneumoniae Electroporation Infectious Diseases Oxaloacetate decarboxylase Biochemistry chemistry biology.protein Recombinant DNA Electrophoresis Polyacrylamide Gel Parasitology Plasmids Transcription Factors |
| Zdroj: | Experimental Parasitology. 115:221-225 |
| ISSN: | 0014-4894 |
| DOI: | 10.1016/j.exppara.2006.08.009 |
| Popis: | A number of peptide tags are available to facilitate the characterization of recombinant proteins. We have tested the bacterial oxaloacetate decarboxylase biotinylation domain for its efficacy in tagging recombinant proteins in vivo in Leishmania. To achieve efficient biotinylation, Leishmania also had to be co-transformed with the gene for bacterial biotin protein ligase (birA gene product). The recombinant chimeric protein could be detected on blots probed with avidin-horseradish peroxidase and purified on immobilized monomeric avidin resins. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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