کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1365955 981577 2006 9 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Development and optimization of a useful assay for determining Hsp90’s inherent ATPase activity
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی آلی
پیش نمایش صفحه اول مقاله
Development and optimization of a useful assay for determining Hsp90’s inherent ATPase activity
چکیده انگلیسی

The Hsp90 molecular chaperone is responsible for the conformational maturation of nascent polypeptides and the rematuration of denatured proteins. Inhibition of Hsp90 represents a promising approach towards the treatment of cancer because numerous signaling cascades can be simultaneously targeted by disruption of the Hsp90-mediated process. Hsp90’s ATPase activity is essential to the Hsp90-mediated protein folding process, consequently, a coupled assay was developed and optimized for determination of Hsp90’s inherent ATPase activity. Using maltose phosphorylase, glucose oxidase, and horseradish peroxidase as components of this assay, a highly reproducible assay with a Z-factor of 0.87 has been produced.

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ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Bioorganic & Medicinal Chemistry - Volume 14, Issue 4, 15 February 2006, Pages 1134–1142
نویسندگان
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