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Lina Wang,Dai Di Fan,Jing He,Zhongcheng Lv,Chen-Hui Zhu 한국생물공학회 2014 Biotechnology and Bioprocess Engineering Vol.19 No.5
Recombinant human full-length mature collagenα1 (III) chain (rhCOL3A1) was secreted by Pichia pastorisGS115, using the Saccharmyces cerevisiae á-mating factorprepro signal, and the theoretical molecular weight ofrhCOL3A1 was 95.344 kDa. The gene cloned from humanplacenta, was designed and cloned into expression vectorpPIC9K under the control of a strong inducible promoterAOX1.The expression stage of rhCOL3A1 was sensitiveto different carbon ratios through mixed fermentation. LCMS/MS analysis and western blotting demonstrated thatthe recombinant human full-length mature collagen α1(III) gene was successfully expressed in P. pastoris GS115during the methanol induction stage. Furthermore, aneffective strategy of mixed fermentation was established toexpress rhCOL3A1 in shake flash. Compared to singlecarbon induction, when induced with mixed carbon at theration of 0.8 (glycerol/methanol), the time corresponding tothe highest yield of rhCOL3A1 (1.27 g/L) was drasticallyreduced by 50%. The same conclusion was observed fromRT-qPCR. Consequently, a new strategy which was moretime-saving and effective was provided for the large-scaleproducing the full-length mature rhCOL3A1.