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Document Type
Thesis - University Access Only
Award Date
1993
Degree Name
Master of Science (MS)
Department / School
Biology and Microbiology
First Advisor
Thomas M. Cheesbrough
Abstract
As stated above, the CPT enzyme is regulated by developmental, environmental, and hormonal signals. To fully elucidate the precise mechanisms responsible for regulation of CPT, it is of interest to develop an expression system for the CPT cDNA. The resulting recombinant protein will be employed for enzymatic characterization and production of antibodies against the CPT antigen. The antibodies will be used to determine if the modulation of CPT occurs at a posttranslational level. Therefore, this study was initiated to accomplish the following objectives: (1) To subclone the CPT cDNA into the pGEMEX-1 expression vector; (2) To develop an E. coli expression system to overproduce the fusion CPT insert; (3) To purify the fusion protein in large quantities for use as an antigen.
Library of Congress Subject Headings
Phosphotransferases
Enzymatic analysis
Fatty acids
Format
application/pdf
Publisher
South Dakota State University
Recommended Citation
Wang, Tie, "Subcloning, Expression, and Purification of Cholinephosphotransferase, A Key Enzyme in Fatty Acid Desaturation in Soybean" (1993). Electronic Theses and Dissertations. 5847.
https://openprairie.sdstate.edu/etd/5847