Page 80 - ebook
P. 80
[A. Biochemistry/Molecular Biology] A-40
Expression of Recombinant human IGF-1 protein in
transgenic Nicotiana benthamiana and Nicotiana tabacum
BY-2 cells
Kwangkyun Park¹, Il-Chul Kim¹, Dong Ju Lee¹,²*
¹Biological Sciences, Chonnam National University, Gwangju 61186, Korea, ²Basic Science Institute, Chonnam
National University, Gwangju 61186, Korea
Human Insulin-like Growth Factor (IGF-1)’s functions of cell proliferation, cell survival, damaged tissue recovery, and
glycemic response have been known as one of the most promising parts in treating growth disorders, diabetes, and
neurodegenerative diseases. Molecular farming is to exploit plant hosts as a recombinant protein expression system
for the sake of the production and utilization of medically valuable proteins. Nicotiana benthamiana and Nicotiana
tabacum BY-2 cells were transformed with Ti plasmid containing a new promoter and the recombinant human IGF-
1 (rhIGF-1) gene. The expression of rhIGF-1 mRNA was detected by RT-PCR (approximately 500 bp) in N.
benthamiana and N. tabacum BY-2 cell. The expressed amount of rhIGF-1 protein was quantified by Western Blot.
The yield of rhIGF-1 was estimated at 0.096~0.11% of the total soluble proteins in transgenic N. benthamiana and
0.034~0.19% in transgenic N. tabacum BY-2 cells. Furthermore, other biomolecular and environmental factors will
be considered and examined to improve the amount of the expressed rhIGF-1, and its activity estimation will be
conducted after the purification process.

