Isolation of a peptide from Ph.D.-C7C phage display library for detection of Cry1Ab
Autor: | Xianjin Liu, Yun Wang, Qian Wang, Ai-hua Wu, Zhen-Ping Hao |
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Rok vydání: | 2017 |
Předmět: |
0301 basic medicine
clone (Java method) Phage display Biophysics Enzyme-Linked Immunosorbent Assay Peptide 02 engineering and technology medicine.disease_cause Biochemistry Hemolysin Proteins 03 medical and health sciences Bacterial Proteins Limit of Detection Peptide Library medicine Bacteriophages Peptide library Molecular Biology chemistry.chemical_classification Bacillus thuringiensis Toxins biology medicine.diagnostic_test Toxin Antibodies Monoclonal Cell Biology 021001 nanoscience & nanotechnology Isolation (microbiology) Molecular biology Endotoxins 030104 developmental biology chemistry Immunoassay biology.protein Antibody Peptides 0210 nano-technology |
Zdroj: | Analytical Biochemistry. 539:29-32 |
ISSN: | 0003-2697 |
DOI: | 10.1016/j.ab.2017.03.004 |
Popis: | Traditional ELISA methods of using animal immunity yield antibodies for detection Cry toxin. Not only is this incredibly harmful to the animals, but is also time-intensive. Here we developed a simple method to yield the recognition element. Using a critical selection strategy and immunoassay we confirmed a clone from the Ph.D-C7C phage library, which has displayed the most interesting Cry1Ab-binding characteristics examined in this study (Fig. 1). The current study indicates that isolating peptide is an alternative method for the preparation of a recognition element, and that the developed assay is a potentially useful tool for detecting Cry1Ab. |
Databáze: | OpenAIRE |
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