|کد مقاله||کد نشریه||سال انتشار||مقاله انگلیسی||ترجمه فارسی||نسخه تمام متن|
|1216524||1494100||2013||9 صفحه PDF||سفارش دهید||دانلود رایگان|
• A novel functional fibrous polymer grafted affinity beads was used for immobilization of l-histidine and Protein L ligands.
• Maximum Igs adsorption capacities of Protein L and l-histidine were found to be 81.8 and 112.3 mg/g, respectively.
• These ligands immobilized affinity beads were used for separation of immunoglobulin from human serum in a batch mode.
• Protein L immobilized affinity beads was provided an efficient purity about 98%.
A novel core shell beaded chromatographic materials was prepared by grafting of glycidyl methacrylate (GMA) on to the surface of poly(hydoxypropyl methacrylate/ethyleneglycol dimethacrylate), p(HPMA/EGDMA) beads via surface-initiated atom transfer radical polymerization (SI-ATRP). For grafting GMA, p(HPMA/EGDMA) beads were first modified with an ATRP initiator. A reaction with 2-bromo-2-methylpropionyl bromide of the hydroxyl groups of the beads led to ATRP initiator-covered surfaces. The grafted p(GMA) fibrous chains on the beads were decorated with two different ligands (i.e., Protein L and l-histidine) for separation of Immunoglobulin's (Igs) from aqueous solution in batch system. The maximum Igs adsorptions on the p(HPMA/EGDMA)-g-p(GMA)-Protein L and p(HPMA/EGDMA)-g-p(GMA)-l-histidine affinity beads were found to be 81.8 and 112.3 mg/g at pH 7.5 and 5.5, respectively. The purity of Igs from human serum was analyzed by HPLC. The Protein L immobilized affinity beads provided purity about 98%. The novel core shell polymeric beads decorated with Protein L showed a good selectivity for Igs molecules from diluted human serum. Adsorption studies of Igs onto Protein L and l-histidine immobilized affinity beads were also carried out in a continuous system.
Journal: Journal of Chromatography B - Volume 936, 1 October 2013, Pages 1–9