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Purification and Glycosylation Pattern of Human L-Ferritin in Pichia pastoris
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  • Purification and Glycosylation Pattern of Human L-Ferritin in Pichia pastoris
  • Purification and Glycosylation Pattern of Human L-Ferritin in Pichia pastoris
저자명
Lee. Jong-Lim,Yang. Seung-Nam,Park. Cheon-Seok,Jeoung. Doo-Il,Kim. Hae-Yeong
간행물명
Journal of microbiology and biotechnology
권/호정보
2004년|14권 1호|pp.68-73 (6 pages)
발행정보
한국미생물생명공학회
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정기간행물|ENG|
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이 논문은 한국과학기술정보연구원과 논문 연계를 통해 무료로 제공되는 원문입니다.
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기타언어초록

Ferritin is an iron storage protein found in most living organisms. For expression and industrial use, human light chain ferritin (L-ferritin) was cloned from human liver cDNA library and expressed in Pichia pastoris strain GS115. The recombinant L-ferritin in Pichia pastoris was glycosylated. In a fed-batch culture, the cell mass reached about 57 g/l of dry cell weight, and the L-ferritin in the cell was increased to about 95 mg/l after 150 h. In an atomic absorption spectrometry analysis, the intracellular content of iron in the L-ferritin transformant was measured as $1,694{pm}85;mu extrm{g}g/g$, which is 5.4-fold more than that of the control strain. This L-ferritin transformant could serve as iron-fortified nutrients in animal feed stock.