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- W2353649335 abstract "The effect of over expression of chaperones SecB and GroEL on the secretion and solubility of protein in Escherichia coli was examined,using a set of the proteins.A diverse range of effects on protein solubility and secretion was observed,and these effects were highly dependent on the particular chaperone.In the host strain over expressing chaperone SecB harboring pSecB,the amount of total periplasmic proteins was increased by about 71% and the activities of alkaline phosphatase(AP) and GL 7 ACA acylase(GL7A) were increased by about 54% and 1.5 fold respectively.In the host strain over expressing chaperone GroEL bearing pGroEL,the amount of total periplasmic proteins was increased by 52%,and the activity of penicillin G acylase(PA)was increased by about 76%;about 90% of Hexameric Calcitonin(Cal6)inclusion body and 15% of MS2 interleukin3(MS2 HIL3)inclusion body became soluble respectively.All the data were compared with the parental strains un bearing plasmids pSecB or pGroEL.In conclusion,the over expression of chaperones SecB and GroEL enhanced the secretion of the proteins,and GroEL also increased the solubility of recombinant proteins." @default.
- W2353649335 created "2016-06-24" @default.
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- W2353649335 date "2000-01-01" @default.
- W2353649335 modified "2023-09-25" @default.
- W2353649335 title "The Effect of Over-expression of Chaperones on the Secretion and the Solubility of Proteins*" @default.
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