The plant peroxidases (EC1.11.17) exit as a large family of isozymes. These isozymes have more than 50% amino acid sequence differences. The function of Wasaba japonica peroxides plays the role as IAA oxidases. The kinetics result shows Wasabia japonica peroxidases displayed affinity (Km = 17.1 £gM) for IAA. The kinetics results in Wasabia japonica peroxidases display affinity (Km = 80.6 £gM) for syringaldazine. LC/MS/MS technique described the data that has proven to be a method for identification and characterization of proteins. The soluble proteins extracted form Wasabia japonica was purified by gel filtration chromatography and two-dimensional gel electrophoresis (2-DE). LC-MS/MS analyses of 2-DE gel spots and identify proteins structure based on the protein fragmentation characteristics. The Mascot Search Results showed that Wasabia japonica peroxidase has a significant similarity (10%) with Arabidopsis thaliana peroxidase.
| Identifer | oai:union.ndltd.org:NSYSU/oai:NSYSU:etd-0212108-142719 |
| Date | 12 February 2008 |
| Creators | Shieh, Chia-lin |
| Contributors | Chin-gme Hsu, Zin -huang Lin, Man-gjye Ger |
| Publisher | NSYSU |
| Source Sets | NSYSU Electronic Thesis and Dissertation Archive |
| Language | English |
| Detected Language | English |
| Type | text |
| Format | application/pdf |
| Source | http://etd.lib.nsysu.edu.tw/ETD-db/ETD-search/view_etd?URN=etd-0212108-142719 |
| Rights | withheld, Copyright information available at source archive |
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