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Information Journal Paper

Title

Thermal stability of recombinant human interferon gamma produced in E. coli

Pages

  57-65

Abstract

 The stability of recombinant proteins has become an increasingly important as more protein therapeutics are developed. In this study, the stability of recombinant human interferon gamma was investigated under storage condition for 0-9 months after production time at 4 and 25℃ . The evaluation of biological activity, covalent dimerization, deamidation and oxidation of protein was done by cell culture, HPLC and SDS-PAGE. The results showed represents that antiviral activity was not decreased at 4℃ but decreased as temperature increased to 25℃ . The inormation rate of deamidated and oxidized forms and covalent dimers at 25℃ was more rapid than 4℃ . Therefore, rhIFN-γ has high stability at 4℃ comparing to 25℃ .

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    APA: Copy

    Maleksabet, Narges, NASIRI KHALILI, MOHAMMAD ALI, & MASOMIAN, MOHAMMAD REZA. (2012). Thermal stability of recombinant human interferon gamma produced in E. coli. JOURNAL OF BIOTECHNOLOGY, 3(1 ), 57-65. SID. https://sid.ir/paper/231173/en

    Vancouver: Copy

    Maleksabet Narges, NASIRI KHALILI MOHAMMAD ALI, MASOMIAN MOHAMMAD REZA. Thermal stability of recombinant human interferon gamma produced in E. coli. JOURNAL OF BIOTECHNOLOGY[Internet]. 2012;3(1 ):57-65. Available from: https://sid.ir/paper/231173/en

    IEEE: Copy

    Narges Maleksabet, MOHAMMAD ALI NASIRI KHALILI, and MOHAMMAD REZA MASOMIAN, “Thermal stability of recombinant human interferon gamma produced in E. coli,” JOURNAL OF BIOTECHNOLOGY, vol. 3, no. 1 , pp. 57–65, 2012, [Online]. Available: https://sid.ir/paper/231173/en

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