• Title/Summary/Keyword: BaekSeungHoCho

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Sang-Seol Lee's manuscript on modern physics in the late 19th century Korea (수학자 보재 이상설(李相卨)의 근대자연과학 수용 - 『백승호초(百勝胡艸)』를 중심으로)

  • Lee, Sang-Gu;Park, Chong-Yun;Kim, Chae Sik;Lee, Jae Hwa
    • Communications of Mathematical Education
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    • v.27 no.4
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    • pp.487-498
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    • 2013

  • Sang-Seol Lee(1870-1917) wrote a manuscript BaekSeungHoCho(百勝胡艸) in the late 19th century. BaekSeungHoCho was transcribed in classical Chinese from the 1879 Japanese book Physics(物理學) by Teizo Ihimori (1851-1916). Sang-Seol Lee, a famous independence activist, is also called Father of the Modern Mathematics Education of Korea, because of his early contribution to the modern mathematics education in the 19th century. In this paper, we introduce contents of his manuscript BaekSeungHoCho for the first time and discuss the significance of this book. Also, we show his contribution on the introduction to modern physics in the late 19th century Korea.

  • https://doi.org/10.7468/jksmee.2013.27.4.487 인용 PDF KSCI

Overproduction of Recombinant Human VEGF (Vascular Endothelial Growth Factor) in Chinese Hamster Ovary Cells

  • Lee, Seong-Baek;Park, Jeong-Soo;Lee, Seung-Hee;Park, Jun-Ho;Yu, Sung-Ryul;Kim, Hee-Chan;Kim, Dong-Jun;Byun, Tae-Ho;Baek, Kwang-Hee;Ahn, Young-Joon;Yoon, Jae-Seung
    • Journal of Microbiology and Biotechnology
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    • v.18 no.1
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    • pp.183-187
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    • 2008

  • Vascular endothelial growth factors (VEGFs) are a family of proteins that mediate angiogenesis. $VEGF_{165}$ is a VEGF-A isoform and has been extensively studied owing to its potential use in therapeutic angiogenesis. This study established Chinese hamster ovary (CHO) cells overexpressing recombinant human $VEGF_{165}$ $(rhVEGF_{165})$ protein. The production rate of the established CHO cells was over 80mg/l of $rhVEGF_{165}$ protein from a 7-day batch culture process using a 7.5-l bioreactor with a 5-l working volume and serum-free medium. The $rhVEGF_{165}$ protein was purified to homogeneity from the culture supernatant using a two-step chromatographic procedure that resulted in a 48% recovery rate. The purified $rhVEGF_{165}$ protein was a glycosylated homodimeric protein with a higher molecular weight (MW) than the protein expressed from insect cells, suggesting that the glycosylation of the $rhVEGF_{165}$ protein in CHO cells differed from that in insect cells. The purified $rhVEGF_{165}$ protein in this study was functionally active with a half-maximal effective concentration of 3.8ng/ml and specific activity of $2.5{\times}10^5U/mg$.

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