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University of Illinois at Urbana-Champaign

Investigation of the Localization, Oligomerization Status, and Binding Activities of Maize Sucrose Synthase

Abstract

dc:description

Recombinant SUS1 C-terminal truncations showed that even the first 50 amino acids of SUS1 could bind to microsomes from kernels as well as to cellulose. The secondary structure of the first 50 amino acids of SUS may be causally involved in the binding activities. Taken together, the results presented in this dissertation gave a better understanding of the dynamic regulation of SUS and documented its specific and vital role in plant metabolism.

Degree

thesis:*
Name thesis:degree_name
Ph.D.
Level thesis:degree_level
Dissertation
Discipline thesis:degree_discipline
Biology
Grantor
University of Illinois at Urbana-Champaign
Year dc:date
2015

Author and committee

dc:creator, dc:contributor.*
Author dc:creator
  • Duncan, Kateri
Contributors dc:contributor
  • Huber, Steven C.

Subjects

dc:subject × 1

Rights

Language dc:language
eng

Identifiers

dc:identifier.*
Identifier
(MiAaPQ)AAI3269883
OAI identifier oai:identifier
oai:www.ideals.illinois.edu:2142/85369

Chain of custody

source
Harvested from
University of Illinois - Urbana-Champaign
Base URL
www.ideals.illinois.edu/oai-pmh
Last updated
2026-07-22
Source record
OAI-PMH GetRecord
citation

Duncan, Kateri. Investigation of the Localization, Oligomerization Status, and Binding Activities of Maize Sucrose Synthase. Dissertation thesis, University of Illinois at Urbana-Champaign, 2015. http://hdl.handle.net/2142/85369