Volume 3, Issue 1 (2012)                   JMBS 2012, 3(1): 57-65 | Back to browse issues page

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Maleksabet N, nasiri khalili M A, masoumian M. Thermal stability of recombinant human interferon gamma produced in E.coli. JMBS 2012; 3 (1) :57-65
URL: http://biot.modares.ac.ir/article-22-7929-en.html
Thermal stability of recombinant human interferon gamma produced in E.coli
Narges Maleksabet * 1, Mohammad ali Nasiri khalili2 , Mohammadreza Masoumian1
1- shahid babaee highway-lavizan-science & biotechnology institute, Tehran
2- Enghelab square-Tehran university- Institute of Biochemistry- Biophysics, Tehran
Abstract:   (11854 Views)
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℃.
Keywords: rh-IFN-γ, Stability, Covalent dimer, Deamidated and oxidized forms
Full-Text [PDF 339 kb]   (5679 Downloads)    
Article Type: _ | Subject: biochemistry|Biotechnology
Received: 2011/10/12 | Accepted: 2012/01/31 | Published: 2012/11/18
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