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《Progress In Biotechnology》 2004-10
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Fermentation and Purification of Secretion Recombinant Human Growth Hormone

HE Zheng xiang 1,2 ZHANG Bu chang 1,2 MA Qing jun 1 ZHANG Yan hong 1 (1 Institute of Biotechnology, Academy of Military Medical Sciences, Beijing 100850, China 2 School of Life Sciences, Anhui University, Hefei 230039, China)  
Engineered pET ompA 3 hGH/BL21(DE3) expressed secretion rhGH by inducing and supplying nutrimental components in 5L fermentor.Expression level of rhGH could reach 250mg/L culture solution by means of selecting components of original culture media,components of supplemental media,volume of supplemental media,the time of supplying supplemental media and supplying speed of supplemental media,secretion rhGH was found to represent 44%~54% of the total proteins in periplasm,and the fermentation time was reduced to 8 hrs.Secretion rhGH was purified in one step with affinity chromatography prepared by the polyclonal antibodies from the rabbit immunized with rhGH,and homogeneous rhGH was obtained,with the purity above 96% identified with reduced and nonreduced SDS PAGE and reversed phase HPLC.The molecular mass size,immunity activity and formation of disulphide bond were identical to those of native hGH.
【CateGory Index】: TQ464
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