چاپ صفحه |  صفحه نخست سامانه |  چکیده مقاله |  نویسندگان |  دانلود مقاله | دانشگاه علوم پزشکی تبریز |
| نویسنده ثبت کننده مقاله | جلال عبدالعلیزاده |
| مرحله جاری مقاله | تایید نهایی |
| دانشکده/مرکز مربوطه | مرکز تحقیقات ایمونولوژی |
| کد مقاله | 58990 |
| عنوان فارسی مقاله | A methodological approach for purification and characterization of human serum albumin |
| عنوان لاتین مقاله | A methodological approach for purification and characterization of human serum albumin |
| ناشر | 6 |
| آیا مقاله از طرح تحقیقاتی و یا منتورشیپ استخراج شده است؟ | بلی |
| عنوان نشریه (خارج از لیست فوق) | |
| نوع مقاله | Original Article |
| نحوه ایندکس شدن مقاله | ایندکس شده سطح یک – ISI - Web of Science |
| آدرس لینک مقاله/ همایش در شبکه اینترنت | http://www.tandfonline.com/doi/pdf/10.1080/15321819.2016.1184163?needAccess=true |
| A methodological approach for purification and characterization of human serum albumin As the most predominant protein in plasma, albumin is synthesized in the liver. Given to various applications of albumin as biopharmaceutical agent, the annual demand for it is 500 tons in the world, which is the highest in the biomedical solutions demand ranking. There exist different procedures for production of albumin. The aim of this study was the purification of human serum albumin (HSA) using immunoaffinity chromatography. After immunization of rabbits, passive immunodiffusion and indirect ELISA tests were applied for assessment of polyclonal antibody production against HSA. Purification was performed by ion exchange chromatography (IEC) and protein G affinity chromatography. The produced anti-HSA IgG was attached to the CNBR-activated Sepharose and applied for albumin purification from human serum. Western blotting (WB) analysis and heat-induced insolubility were performed for functional and stability measurement assessment of immunoaffinity purified HSA, respectively. The optimum titer of anti-HSA determined by indirect ELISA was 256000. The SDS-PAGE showed that the purity rate of albumin was approximately 98% and WB confirmed the HSA functionality. Also, the heat-induced insolubility of immunoaffinity purified HSA was the same as the commercial HSA. Affinity chromatography using produced polyclonal antibody would be a robust method for purification of HSA. |
| نویسنده | نفر چندم مقاله |
|---|---|
| جلال عبدالعلیزاده | ششم |
| رامین رئوفی نیا | اول |
| لیلی عاقبتی | چهارم |
| نام فایل | تاریخ درج فایل | اندازه فایل | دانلود |
|---|---|---|---|
| A methodological approach for purification and characterization of human serum albumin.pdf | 1395/07/18 | 1265056 | دانلود |
| A methodological approach for purification and characterization of human serum albumin.pdf | 1395/07/18 | 1265056 | دانلود |
