Abstract
A recombinant CHO cell line in which the expresison of human follicle stimulating hormone (hFSH) was under the control of the β 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/106 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.
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Chotigeat, W., Watanapokasin, Y., Mahler, S. et al. Role of environmental conditions on the expression levels, glycoform pattern and levels of sialyltransferase for hFSH produced by recombinant CHO cells. Cytotechnology 15, 217–221 (1994). https://doi.org/10.1007/BF00762396
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DOI: https://doi.org/10.1007/BF00762396