Title page for etd-0212108-142719


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URN etd-0212108-142719
Author Chia-lin Shieh
Author's Email Address charlene.shieh@scinopharm.com.tw
Statistics This thesis had been viewed 5583 times. Download 1834 times.
Department Biological Sciences
Year 2007
Semester 2
Degree Master
Type of Document
Language English
Title The biochemical studies of peroxidase in Wasabia japonica
Date of Defense 2008-01-12
Page Count 34
Keyword
  • LC-MS/MS
  • Wasabia japonica
  • peroxidase
  • Abstract 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 μM) for IAA. The kinetics results in Wasabia japonica peroxidases display affinity (Km = 80.6 μM) 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.
    Advisory Committee
  • Chin-gme Hsu - chair
  • Man-gjye Ger - co-chair
  • Zin -huang Lin - advisor
  • Files
  • etd-0212108-142719.pdf
  • indicate accessible in a year
    Date of Submission 2008-02-12

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