Isolation and characterization of a 30 kDa protein with antifungal activity from leaves of Engelmannia pinnatifida
| Autor: | Q K Huynh, Dilip M. Shah, C E Smith, J R Borgmeyer, L D Bell |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
Antifungal Agents
Molecular Sequence Data Microbial Sensitivity Tests Biology Biochemistry Petunia chemistry.chemical_compound Residue (chemistry) Ammonium Amino Acid Sequence Ribonuclease Molecular Biology Peptide sequence Chromatography High Pressure Liquid Plant Proteins chemistry.chemical_classification Sequence Homology Amino Acid Fungi Cell Biology Plants Chromatography Ion Exchange biology.organism_classification Yeast Plant Leaves Engelmannia pinnatifida chemistry Chromatography Gel biology.protein Electrophoresis Polyacrylamide Gel Glycoprotein Research Article |
| Zdroj: | Biochemical Journal. 316:723-727 |
| ISSN: | 1470-8728 0264-6021 |
| Popis: | During the course of screening plants for novel antifungal activity, we found that a high-molecular-mass fraction of an extract from leaves of Engelmannia pinnatifida exhibited potent and broad-spectrum antifungal activity. In this study a 30 kDa protein from E. pinnatifida leaves was purified to homogeneity by ammonium sulphate precipitation, gel filtration, Mono-Q and C18 reverse-phase column chromatographies. The purified protein showed potent antifungal activity against various plant pathogens with as little as 50 ng. The N-terminal amino acid sequence of the purified protein was determined as XXTKFDFFTLALQXPAXF, where X indicates an unidentified residue. This sequence showed 35–50% sequence identity with purified style glycoproteins associated with self-incompatibility from wild tomato, tobacco and petunia, a phosphate-starvation-induced ribonuclease from cultured tomato cells and the SIR 63.4 kDa protein from yeast. |
| Databáze: | OpenAIRE |
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