Deepak, A. V. and Thippeswamy, G. and Shivakameshwari, M. N. and Bharathi P. Salimath (2003) Isolation and characterization of a 29-kDa glycoprotein with antifungal activity from bulbs of Urginea indica. Biochemical and Biophysical Research Communications, 311 (3). 735 - 742. ISSN 1090-2104
Full text not available from this repository. (Request a copy)Abstract
In this study an antifungal protein from Urginea indica bulbs was purified to homogeneity by acid precipitation, Diol 300 Gel-filtration, and C18 reverse phase HPLC. Its molecular mass was estimated to be 29kDa and periodic acid–Schiff (PAS) staining showed that identified antifungal molecule is a glycoprotein. The neutralization of antifungal activity after periodate oxidation of 29kDa glycoprotein suggests that the glycan part of the molecule appears to be involved in antifungal activity. N-terminal amino acid sequence of the purified protein was determined as SQLKAXIXDF. This sequence had no sequence similarity with any antifungal proteins. A polyclonal antiserum was raised against purified protein and used in immunolocalization analysis. Results suggest that it is localized to the cell wall of the bulb. Antifungal tests have demonstrated that U. indica protein exerts a fungistatic effect. It completely inhibits the germination of spores and hyphal growth of Fusarium oxysporum.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | , Cell wall, Antifungal glycoprotein, |
| Subjects: | B Life Science > Botany |
| Divisions: | Department of > Zoology |
| Depositing User: | LA manjunath user |
| Date Deposited: | 04 Sep 2019 11:54 |
| Last Modified: | 16 Nov 2019 10:24 |
| URI: | http://eprints.uni-mysore.ac.in/id/eprint/7582 |
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