Dye-ligand and metal chelate poly(2-hydroxyethylmethacrylate) membranes for affinity separation of proteins
Yükleniyor...
Tarih
1998
Yazarlar
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Elsevier Science Bv
Erişim Hakkı
info:eu-repo/semantics/closedAccess
Özet
Cibacron Blue F3GA was covalently immobilized onto poly(2-hydroxyethyl methacrylate) (pHEMA) membranes via the nucleophilic reaction between the chloride of its triazine ring and the hydroxyl group of pHEMA. Then, Fe3+ ions were complexed by chelation with the immobilized Cibacron Blue F3GA molecules. Different amounts of Fe3+ ions were loaded on the membranes by changing the concentration of Fe3+ ions and pH of the reaction medium. Membranes with or without Fe3+ were used in the adsorption of glucose oxidase, catalase and bovine serum albumin. The adsorption capacities of these membranes were determined by changing pH and the concentration of the proteins in the adsorption medium. The adsorption phenomena appeared to follow a typical Langmuir isotherm. The maximum capacities (q(m)) of the Fe3+ complexed membranes for glucose oxidase, catalase and bovine serum albumin (8.70.10(-3) mu mol m(-2), 2.15.10(-3) mu mol m(-3) and 2.21.10(-3) mu mol m(-2)) were greater than those of the untreated membranes (6.79.10(-3) mu mol m(-2), 1.34.10(-3) mu mol m(-2) and 1.94.10(-3) mu mol m(-2)) respectively. The nonspecific adsorption of the enzymes and the protein on the pHEMA membranes was negligible. (C) 1998 Elsevier Science B.V.
Açıklama
Anahtar Kelimeler
affinity membranes, membranes, metal chelate affinity chromatography, poly(2-hydroxyethyl methacrylate) membranes, affinity adsorbents, proteins, enzymes, metal chelates, iron, cibacron blue F3GA
Kaynak
Journal Of Chromatography A
WoS Q Değeri
Q1
Scopus Q Değeri
Q1
Cilt
799
Sayı
1-2
Künye
closedAccess
