원문정보
초록
영어
Recombinant human cytotoxic T-lymphocyte antigen 4-immunoglobuline (hCTLA4Ig) was produced by recombinant Chinese hamster ovary (rCHO) cells using 125-mL erlenmyler flasks. Mammalian cells produce relatively low level of recombinant proteins compared with microbial cells. The use of sodium butyrate in cell cultures has been known to enhance specific genes controlled by several promoters. Many reports have described significant increase of recombinant
proteins in the presence of 0.5-4 mM sodium butyrate. Lowering temperature below 37℃ has also been considered as an effective tool for increasing specific productivity of recombinant protein. Unlike the specific growth rate, effect of low temperature on specific productivity still remains unclear. We investigated the combination effects of the addition of optimum concentration of sodium butyrate and optimal temperature shift on hCTLA4Ig specific productivity in rCHO cells. When viable cell density was reached at maximum level, 1 mM sodium butyrate was added to the culture medium and culture temperature was shifted to 34℃. Simultaneous application of sodium butyrate and temperature shift enhanced specific productivity up to
1.5-fold. Therefore, these results suggest that the specific productivity of hCTLA4Ig became higher because of the simultaneous application of sodium butyrate and temperature shift.