کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1988092 | 1540329 | 2006 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Use of the myosin motor domain as large-affinity tag for the expression and purification of proteins in Dictyostelium discoideum
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کلمات کلیدی
PBSMBPGSTARP1Dynein intermediate chainPMSFDynein heavy chainDictyostelium discoideumTLCKTPCKTev - به توTame - تامSaccharomyces cerevisiae - ساکارومایسس سرویزیهphenylmethyl sulfonyl fluoride - فنیل متیل سولفونیل فلورایدPhosphate-buffered saline - محلول نمک فسفات با خاصیت بافریMus musculus - نام علمی انسانHomo sapiens - نام علمی انسانTobacco etch virus - ویروس تنباکو اچmaltose binding protein - پروتئین متصل به مالتوزglutathione S-transferase - گلوتاتیون S-ترانسفراز
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Use of the myosin motor domain as large-affinity tag for the expression and purification of proteins in Dictyostelium discoideum Use of the myosin motor domain as large-affinity tag for the expression and purification of proteins in Dictyostelium discoideum](/preview/png/1988092.png)
چکیده انگلیسی
The cellular slime mold Dictyostelium discoideum is increasingly be used for the overexpression of proteins. Dictyostelium is amenable to classical and molecular genetic approaches and can easily be grown in large quantities. It contains a variety of chaperones and folding enzymes, and is able to perform all kinds of post-translational protein modifications. Here, new expression vectors are presented that have been designed for the production of proteins in large quantities for biochemical and structural studies. The expression cassettes of the most successful vectors are based on a tandem affinity purification tag consisting of an octahistidine tag followed by the myosin motor domain tag. The myosin motor domain not only strongly enhances the production of fused proteins but is also used for a fast affinity purification step through its ATP-dependent binding to actin. The applicability of the new system has been demonstrated for the expression and purification of subunits of the dynein-dynactin motor protein complex from different species.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 39, Issues 1â3, 15 August 2006, Pages 37-44
Journal: International Journal of Biological Macromolecules - Volume 39, Issues 1â3, 15 August 2006, Pages 37-44
نویسندگان
Martin Kollmar,