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Synthesis and use of protein G imprinted cryogel as affinity matrix to purify protein G from cell lyaste.

By Sevgi Asliyuce Coban, Bo Mattiasson and Gashaw Mamo

Abstract

Monolithic macroporous cryogel imprinted with protein G was prepared using a functional co-monomer of N-methacryloyl-l-phenylalanine and 2-hydroxyethyl methacrylate. The chemical structure of the cryogel prepared was studied by FTIR-spectroscopy and its porosity was analysed using scanning electron microscopy. The cryogel was used to purify protein G from recombinant Escherichia coli cell lysate and the effect of pH, temperature, ionic strength, flow rate, etc on the adsorption of protein G to the monolithic column have been investigated. The selectivity of the imprinted cryogel was studied using protein A and myoglobin. It was possible to capture about 9mg of Protein G per g of the cryogel

Topics: Structural Biology
Publisher: 'Elsevier BV'
Year: 2016
DOI identifier: 10.1016/j.jchromb.2015.12.060
OAI identifier: oai:lup.lub.lu.se:feeaeb3c-e780-42ab-9885-f809427c4429
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