Chotigeat W, Watanapokasin Y, Mahler S, Gray P P
Department of Biotechnology, University of New South Wales, Sydney, Australia.
Cytotechnology. 1994;15(1-3):217-21. doi: 10.1007/BF00762396.
A recombinant CHO cell line in which the expression of human follicle stimulating hormone (hFSH) was under the control of the beta actin promoter was maintained in steady state perfusion cultures on a protein free medium. The level of expression of the hFSH was controlled by varying the steady state level of dissolved oxygen (10-90% of air saturation) and of sodium butyrate (0-1.5mM). Under these conditions, the specific productivity of hFSH (qFSH) varied from 0.7 to 4.8 ng hFSH/10(6) cells/h. As the specific productivity of hFSH increased, there was a shift in the FSH isoforms to the lower pI fractions, corresponding to increased sialic acid content. As the specific productivity of hFSH increased, shifting the isoform distribution towards the lower pI isoforms, that the sialyltransferase enzymic activity also increased.
一种重组CHO细胞系，其中人促卵泡激素（hFSH）的表达受β-肌动蛋白启动子控制，该细胞系在无蛋白培养基的稳态灌注培养中维持。通过改变溶解氧（空气饱和度的10-90%）和丁酸钠（0-1.5mM）的稳态水平来控制hFSH的表达水平。在这些条件下，hFSH的比生产率（qFSH）在0.7至4.8 ng hFSH/10(6)细胞/小时之间变化。随着hFSH比生产率的增加，FSH同工型向较低pI组分转移，这对应于唾液酸含量的增加。随着hFSH比生产率的增加，同工型分布向较低pI同工型转移，唾液酸转移酶活性也增加。
