Ring‐opening metathesis polymerization‐derived,lectin‐functionalized monolithic supports for affinity separation of glycoproteins |
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Authors: | Rajendar Bandari Jürgen Kuballa Michael R Buchmeiser |
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Institution: | 1. Lehrstuhl für Makromolekulare Stoffe und Faserchemie, Institut für Polymerchemie, Universit?t Stuttgart, , Stuttgart, Germany;2. Galab Laboratories GmbH, , Geesthacht, Germany;3. Institut für Textilchemie und Chemiefasern (ITCF), , Denkendorf, Germany |
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Abstract: | Lectin‐functionalized monolithic columns were prepared within polyether ether ketone (PEEK) columns (150 × 4.6 mm id) via transition metal‐catalyzed ring‐opening metathesis polymerization of norborn‐2‐ene (NBE) and trimethylolpropane‐tris(5‐norbornene‐2‐carboxylate) (CL) using the first‐generation Grubbs initiator RuCl2(PCy3)2(CHPh) (1, Cy = cyclohexyl) in the presence of a macro‐ and microporogen, i.e. of 2‐propanol and toluene. Postsynthesis functionalization was accomplished via in situ grafting of 2,5‐dioxopyrrolidin‐1‐yl‐bicyclo2.2.1]hept‐5‐ene‐2‐carboxylate to the surface of the monoliths followed by reaction with α,ω‐diamino‐poly(ethyleneglycol). The pore structure of the poly(ethyleneglycol)‐ derivatized monoliths was investigated by electron microscopy and inverse‐size exclusion chromatography, respectively. The amino‐poly(ethyleneglycol) functionalized monolithic columns were then successfully used for the immobilization of lectin from Lens culinaris hemagglutinin. The thus prepared lectin‐functionalized monoliths were applied to the affinity chromatography‐based purification of glucose oxidase. The binding capacity of Lens culinaris hemagglutinin‐immobilized monolithic column for glucose oxidase was found to be 2.2 mg / column. |
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Keywords: | Bioseparation Glycoproteins Lectin affinity chromatography Monolith ROMP |
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