Biochemical and Molecular Approaches to Characterizing the Myrosinase Enzyme System in Horseradish (Armoracia Rusticana)
Li, Xian
This item is only available for download by members of the University of Illinois community. Students, faculty, and staff at the U of I may log in with your NetID and password to view the item. If you are trying to access an Illinois-restricted dissertation or thesis, you can request a copy through your library's Inter-Library Loan office or purchase a copy directly from ProQuest.
Permalink
https://hdl.handle.net/2142/83099
Description
Title
Biochemical and Molecular Approaches to Characterizing the Myrosinase Enzyme System in Horseradish (Armoracia Rusticana)
Author(s)
Li, Xian
Issue Date
2004
Doctoral Committee Chair(s)
Kushad, Mosbah M.
Department of Study
Natural Resrouces and Environmental Sciences
Discipline
Natural Resrouces and Environmental Sciences
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Agriculture, Food Science and Technology
Language
eng
Abstract
A full length cDNA (ArM1) encoding myrosinase was cloned from horseradish root by RACE-PCR. ArM1 has an open reading frame of 1,614 nucleotides with a deduced protein of 538 amino acid and molecular mass of 61.6 kDa. Heterologous expression of ArM1 in Spodoptera frugiperda insect cells resulted in an immune active myrosinase protein product and gave rise to a band of approximately 66 kDa in western blot analysis. ArM1 has the highest overall amino acid identity (72%) with Arabidopsis thaliana myrosinase TGG2. Phylogenetic analysis shows that ArM1 gene does not cluster with any of the currently known myrosinase subfamily and it may represent another myrosinase subfamily in root tissue.
Use this login method if you
don't
have an
@illinois.edu
email address.
(Oops, I do have one)
IDEALS migrated to a new platform on June 23, 2022. If you created
your account prior to this date, you will have to reset your password
using the forgot-password link below.