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- W2393827731 abstract "Pichia Pastoris is one of the most successful heterologous protein expression systems until now.It doesn't have the endotoxic problem which always existed in the prokaryotic expression system nor the viral contamination of recombinant proteins produced in mammalian cells culture.Furthermore,unlike bacteria,yeasts can carry out the similar post-translational protein processing as higher eukaryotes,such as signal peptide cleavage,disulfide bonds formation and the glycosylation.However,it is not clear which protease may present in the culture media and degrade heterologous protein which leads poor yield of protein of interest.Objective:Comparing the GS115 proteomics differences cultured in different carbon source media to optimize the heterologous protien expression system.Methods:By using LC-ESI-MS/MS combined with Griffin's new calculation method,intracellular and supernatant protein profiling and protein abundance of GS115 in 4 different carbon source media were identified and compared.Results:Intracellular and supernatant protein profiling and related protein abundance of GS115 in 4 different carbon source media were obtained with LC-ESI-MS/MS analysis and Label-free normalized quantification method.Conclusions:The findings will be helpful to develop novel strains which may optimize the Pichia pastoris heterologous protein expression system." @default.
- W2393827731 created "2016-06-24" @default.
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- W2393827731 date "2012-01-25" @default.
- W2393827731 modified "2023-09-25" @default.
- W2393827731 title "Proteomic Analysis of Pichia pastoris GS115 Cultured in Different Carbon Source Mediums" @default.
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