کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1208785 | 965318 | 2006 | 9 صفحه PDF | دانلود رایگان |
A chromatographic method to purify decorin core protein from human lung tissue is described. The method is simple and rapid, using a combination of two-anion exchange and one reversed phase chromatography steps and the enzymatic digestion with chondroitinase ABC. Approximately 170 μg decorin core protein were purified from 25 g of lung tissue with an enrichment factor of 1800-fold relative to the initial protein content. SDS-PAGE analysis of the final product revealed a single 42 kDa protein band, which was recognized by anti-decorin antibodies upon Western blotting and identified by mass spectrometry. Further digestion with PNGase F evidenced the presence of three N-linked oligosaccharides on the core protein. This method forms the basis for studying structural alterations of decorin related to the pathology of diseases where tissue destruction plays a role.
Journal: Journal of Chromatography A - Volume 1123, Issue 2, 11 August 2006, Pages 151–159