Cell lines derived from mammalian are dominant systems for the production of recombinant therapeutic\r\nproteins because of their capacity for correct protein folding, assembly and post-translational modification.\r\nIn the search of an efficient method for the production of a recombinant protein using animal cell culture, we\r\ninvestigated the effects of different treatment including fetal calf serum concentration, glycerol and culture\r\ntemperature on a Chinese hamster ovary (CHO) cell line on the production of recombinant human growth\r\nhormone (rhGH) and recombinant Chinese hamster ovary (rCHO) viability. The GH production was\r\nassessed using ELISA and western blotting methods and cell viability was determined by flow cytometry.\r\nThe production of recombinant protein increased by 2-fold when stimulatory chemical such as glycerol was\r\nadded in two stages, first cells were cultured without glycerol for a period of time in order to obtain enough\r\ncell density and then glycerol was added to achieve high specific productivity.. Moreover, glycerol addition\r\nincreased cell viability. Low culture temperature (below 37�ºC) led to enhanced cellular productivity of the\r\nrhGH by 3-fold but decreased cell viability. These findings indicate that quite simple factors such as culture\r\ntemperature and addition of simple chemicals may lead to the improvement of industrial process for the\r\nproduction of recombinant proteins such as rhGH.
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