Purification and Glycosylation Pattern of Human L-Ferritin in Pichia pastoris
2004
Lee, J.L. (Kyung Hee University, Suwon, Republic of Korea) | Jeoung, D.I. (Kangwon National University, Chuncheon, Republic of Korea) | Yang, S.N. (Kyung Hee University, Suwon, Republic of Korea) | Park, C.S. (Kyung Hee University, Suwon, Republic of Korea) | Kim, H.Y. (Kyung Hee University, Suwon, Republic of Korea), E-mail: [email protected]
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±85 μg/g, which is 5.4-fold more than that of the control strain.
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