کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2488053 | 1114451 | 2006 | 13 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Biophysical Comparability of the Same Protein From Different Manufacturers: A Case Study Using Epoetin Alfa From Epogen® and Eprex®
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
epoetin alfaUV/Vis spectroscopy - UV / Vis spectroscopyerythropoietin - اریتروپویتینcircular dichroism - رنگ تابی دورانیProtein conformation - سازگاری پروتئینanalytical ultra-centrifugation - سانتریفوژ فوق العاده تحلیلیFluorescence spectroscopy - فوتولومینسانس یا فلوئورسانس یا فسفرسانسcomparability - قابلیت مقایسهprotein folding/refolding - پروتئین تاشو / انجمادGlycoprotein - گلیکوپروتئین
موضوعات مرتبط
علوم پزشکی و سلامت
داروسازی، سم شناسی و علوم دارویی
اکتشاف دارویی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
This study focuses on the development and application of biophysical methodology to characterize conformations of Epogen® and Eprex®, the injectable formulations of recombinant human Epoetin alfa produced by different manufacturers and commonly used for the treatment of renal anemia. In these studies Eprex, from prefilled syringes, and Epogen bulk product formulated in a buffer similar to the Eprex formulation, were purified by anion-exchange chromatography. Analytical ultracentrifugation studies of the purified main peak from each sample demonstrated that Epogen contains a single component with an s value of 2.51 while Eprex contains a single component with the same molecular weight but with an s value of 2.44 suggesting a slight difference in hydrodynamic structure. The degree of α-helicity was compared by far-UV circular dichroism and shown to contain slight differences. Intrinsic tryptophan fluorescence and near-UV circular dichroism were assessed and demonstrated additional differences between the proteins. Finally, the global stability of the proteins was monitored using thermal unfolding monitored by far-UV circular dichroism. The Epoetin alfa of Epogen demonstrated complete reversibility while the Epoetin alfa purified from Eprex demonstrated only 80%-85% thermal reversibility when heated to 100°C. Together the data indicate that the proteins are not structurally identical.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Pharmaceutical Sciences - Volume 95, Issue 9, September 2006, Pages 1931-1943
Journal: Journal of Pharmaceutical Sciences - Volume 95, Issue 9, September 2006, Pages 1931-1943
نویسندگان
Songpon Deechongkit, Kenneth H. Aoki, Sungae S. Park, Bruce A. Kerwin,