کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9028204 | 1561659 | 2005 | 4 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Purification of transgenic plant-derived recombinant human acetylcholinesterase-R
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم محیط زیست
بهداشت، سم شناسی و جهش زایی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Purification of transgenic plant-derived recombinant human acetylcholinesterase-R Purification of transgenic plant-derived recombinant human acetylcholinesterase-R](/preview/png/9028204.png)
چکیده انگلیسی
Nicotiana benthamiana plants were engineered to express a codon-optimized gene encoding the human acetylcholinesterase-R (AChE) isoform. The transgenic plants expressed the protein at >0.4% of total soluble protein, and the plant-produced enzyme was purified to homogeneity. Following lysis, procainamide affinity chromatography and anion-exchange chromatography, more than 400-fold purification was achieved and electrophoretic purity was obtained. This pure protein is kinetically indistinguishable from the only commercially available source of human acetylcholinesterase, which is produced in mammalian cell culture. Thus, we have demonstrated a model system for the production of acetylcholinesterase, which is not susceptible to the quantitative limitations or mammalian pathogens associated with purification from mammalian cell culture or human serum.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Chemico-Biological Interactions - Volumes 157â158, 15 December 2005, Pages 331-334
Journal: Chemico-Biological Interactions - Volumes 157â158, 15 December 2005, Pages 331-334
نویسندگان
Brian C. Geyer, Mrinalini Muralidharan, Irene Cherni, Jeffrey Doran, Samuel P. Fletcher, Tama Evron, Hermona Soreq, Tsafrir S. Mor,