کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8360514 | 1542340 | 2014 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
High level expression, efficient purification, and bioactivity of recombinant human metallothionein 3 (rhMT3) from methylotrophic yeast Pichia pastoris
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
Metallothionein 3 (MT3) is an important biochemical mediator regulating many physiological and pathophysiological processes including neuron cell protection, privation of reactive oxygen species-induced DNA damage, and protection against light induced retinal damage. In this study, a human gene encoding for MT3 with c-terminal extension of His6-tag was inserted into vector pPICZaA, and overexpressed in Pichia pastoris strain X-33. The rhMT3 was purified by one step Ni+-NTA affinity chromatography yielding 270Â mg/L of over 90% purity. Functional analysis of the purified rhMT3 using inductively coupled plasma mass spectrometry demonstrated that it has biological function, binding with metal ions Cd2+, Cu2+ and Zn2+. In summary, the experimental procedure we have developed facilitates production of large amounts of an active rhMT3 for further research and drug development.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Protein Expression and Purification - Volume 101, September 2014, Pages 121-126
Journal: Protein Expression and Purification - Volume 101, September 2014, Pages 121-126
نویسندگان
Qi Wu, Bin Li, Fei Wu, Lijun Yang, Shiwu Li, Hongbo Li, Donghai Wu, Taixing Cui, Dongqi Tang,