Adsorption and separation of proteins on composite anion exchangers with poly(N-diethylaminoethylacrylamide) bonded phases

Autor:	Vitali P. Zubov, Alexander E. Ivanov
Rok vydání:	1994
Předmět:	chemistry.chemical_classification Acrylate Chromatography biology Organic Chemistry Composite number General Medicine Polymer Biochemistry Analytical Chemistry Ion chemistry.chemical_compound Adsorption chemistry Desorption Excluded volume biology.protein Bovine serum albumin
Zdroj:	Journal of Chromatography A. 673:159-165
ISSN:	0021-9673
DOI:	10.1016/0021-9673(94)85034-8
Popis:	Composite anion exchangers for chromatography of proteins were prepared by chemical adsorption of poly( p -nitrophenyl acrylate) on γ-aminopropylsilicas followed by coupling of the esters to 2-diethylaminoethylamine. Separation of standard proteins (bovine serum albumin and ovalbumin) on these anion exchangers established their enhanced selectivity and milder desorption conditions as compared with polyethyleneiminesilicas and DEAE-Toyopearl 650M. Frontal analysis was used to evaluate the maximum binding capacity for ovalbumin adsorption on the new packing, which was found to be 13 mg/ml and so nearly half those observed with polyethyleneiminesilicas of comparable pore diameter. The possible role of the excluded volume of the attached polymer is discussed with respect to the adsorptivity of the composite ion exchangers.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::d83483d396b56da363c4fb21fa0033c7 https://doi.org/10.1016/0021-9673(94)85034-8 Zobrazit plný text záznamu